|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
78-483 |
0e+00 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 760.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 78 VPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQD- 156
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 157 ----SLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTDSVSS 232
Cdd:PLN02528 81 rsdsLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 233 EHAVIGGD-----SVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHT 307
Cdd:PLN02528 161 EEATIAEQeefstSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 308 FLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKL 387
Cdd:PLN02528 241 FLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 388 NPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQ 467
Cdd:PLN02528 321 NPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNE 400
|
410
....*....|....*.
gi 75186155 468 WKEYVEKPELLMLQMR 483
Cdd:PLN02528 401 WKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
268-479 |
1.03e-93 |
|
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: 282.89 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 268 MTMA-TSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIG 346
Cdd:pfam00198 1 MTESkQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 347 VAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGR 426
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 75186155 427 IEKVPKFsKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLM 479
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
63-480 |
3.24e-65 |
|
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: 219.75 E-value: 3.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 63 SNEAMATDS-NSGLIDVPLAQTGeGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIK 141
Cdd:TIGR01348 103 QAQAAPAAGqSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 142 VGETLVRLAVEDS--------------QDSLLTTDSSEIVTLGGSKQGTENLLGALS---------TPAVRNLAKDLGID 198
Cdd:TIGR01348 182 TGDLILTLSVAGStpatapapasaqpaAQSPAATQPEPAAAPAAAKAQAPAPQQAGTqnpakvdhaAPAVRRLAREFGVD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 199 INVITGTGKDGRVLKEDVLRFSDQKGFVTDSvSSEHAVIGGDSVSTKASSNFED----KTVPLRGFSRAMVKTMTMA-TS 273
Cdd:TIGR01348 262 LSAVKGTGIKGRILREDVQRFVKEPSVRAQA-AAASAAGGAPGALPWPNVDFSKfgevEEVDMSRIRKISGANLTRNwTM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 274 VPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEH 353
Cdd:TIGR01348 341 IPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPN 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 354 GLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKF 433
Cdd:TIGR01348 421 GLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 75186155 434 SKEGTVyPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLML 480
Cdd:TIGR01348 501 NGKEFE-PRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
76-149 |
2.28e-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: 95.93 E-value: 2.28e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75186155 76 IDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
76-150 |
4.02e-22 |
|
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: 89.74 E-value: 4.02e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75186155 76 IDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLA 150
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
78-483 |
0e+00 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 760.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 78 VPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQD- 156
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 157 ----SLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTDSVSS 232
Cdd:PLN02528 81 rsdsLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 233 EHAVIGGD-----SVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHT 307
Cdd:PLN02528 161 EEATIAEQeefstSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 308 FLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKL 387
Cdd:PLN02528 241 FLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 388 NPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQ 467
Cdd:PLN02528 321 NPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNE 400
|
410
....*....|....*.
gi 75186155 468 WKEYVEKPELLMLQMR 483
Cdd:PLN02528 401 WKSYVEKPELLMLHMR 416
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
84-480 |
7.41e-126 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 372.20 E-value: 7.41e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 84 GEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDS------ 157
Cdd:PRK11856 11 GEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAaaaaea 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 158 ----------LLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKgfvt 227
Cdd:PRK11856 91 apeapapepaPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAA---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 228 dsvSSEHAVIGGDSVSTKASSNFEDKTVPLRGFSRAMVKTMTMATS-VPHFHFVEEINCDSLVELKQFFKENNtdstIKH 306
Cdd:PRK11856 167 ---APAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKReIPHFTLTDEVDVTALLALRKQLKAIG----VKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 307 TFLPTLIKSLSMALTKYPFVNSCFNAEslEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNK 386
Cdd:PRK11856 240 TVTDFLIKAVALALKKFPELNASWDDD--AIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 387 LNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFsKEGTVYPASIMMVNIAADHRVLDGATVARFCC 466
Cdd:PRK11856 318 LKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLSLSFDHRVIDGADAARFLK 396
|
410
....*....|....
gi 75186155 467 QWKEYVEKPELLML 480
Cdd:PRK11856 397 ALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
68-480 |
1.96e-118 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 357.98 E-value: 1.96e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 68 ATDSNSGLIDVPLAQTGEgIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLV 147
Cdd:PRK11855 112 AAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 148 RLAVEDSQDSLLTTDSSEIV---------------TLGGSKQGTENLLG---ALSTPAVRNLAKDLGIDINVITGTGKDG 209
Cdd:PRK11855 191 VIEVAAAAPAAAAAPAAAAPaaaaaaapapapaaaAAPAAAAPAAAAAPgkaPHASPAVRRLARELGVDLSQVKGTGKKG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 210 RVLKEDVLRFsdQKGFVTDSVSSEHAVIGGDSVSTKAS-------SNF-EDKTVPLRGFSRAMVKTMTMA-TSVPHFHFV 280
Cdd:PRK11855 271 RITKEDVQAF--VKGAMSAAAAAAAAAAAAGGGGLGLLpwpkvdfSKFgEIETKPLSRIKKISAANLHRSwVTIPHVTQF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 281 EEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNI 360
Cdd:PRK11855 349 DEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 361 KNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPkFSKEGTVY 440
Cdd:PRK11855 429 KDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKEFV 507
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 75186155 441 PASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLML 480
Cdd:PRK11855 508 PRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
268-479 |
1.03e-93 |
|
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: 282.89 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 268 MTMA-TSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIG 346
Cdd:pfam00198 1 MTESkQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 347 VAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGR 426
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 75186155 427 IEKVPKFsKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLM 479
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
182-478 |
2.67e-70 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 225.83 E-value: 2.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 182 ALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKgfvTDSVSSEHAVIGGDSVSTKASSN----------FE 251
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSL---KSAPTPAEAASVSSAQQAAKTAApaaappklegKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 252 DKTVPLRgfsRAMVKTMTMA-TSVPHFHFVEEINCDSLVELKQFFKENNTDST-IKHTFLPTLIKSLSMALTKYPFVNSC 329
Cdd:PRK11857 79 EKVAPIR---KAIARAMTNSwSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEgVKLTFLPFIAKAILIALKEFPIFAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 330 FNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKF 409
Cdd:PRK11857 156 YDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75186155 410 GSPLLNLPEVAIIALGRIEKVPkFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELL 478
Cdd:PRK11857 236 GVPVINYPELAIAGVGAIIDKA-IVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
86-464 |
1.56e-67 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 227.96 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 86 GIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDSLLTTDSSE 165
Cdd:PRK11854 215 GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 166 IV-----------------TLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTD 228
Cdd:PRK11854 295 AApapaaakaeapaaapaaKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 229 SVSSEHAVIGGD----SVSTKASSNFED-KTVPL---RGFSRA-MVKTMTMATSVPHFHFVEeincdsLVELKQFFKENN 299
Cdd:PRK11854 375 AAPAAAAAGGGGpgllPWPKVDFSKFGEiEEVELgriQKISGAnLHRNWVMIPHVTQFDKAD------ITELEAFRKQQN 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 300 -----TDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKE 374
Cdd:PRK11854 449 aeaekRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 375 LSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKF-SKEgtVYPASIMMVNIAADH 453
Cdd:PRK11854 529 LMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWnGKE--FAPRLMLPLSLSYDH 606
|
410
....*....|.
gi 75186155 454 RVLDGATVARF 464
Cdd:PRK11854 607 RVIDGADGARF 617
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
63-480 |
3.24e-65 |
|
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: 219.75 E-value: 3.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 63 SNEAMATDS-NSGLIDVPLAQTGeGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIK 141
Cdd:TIGR01348 103 QAQAAPAAGqSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 142 VGETLVRLAVEDS--------------QDSLLTTDSSEIVTLGGSKQGTENLLGALS---------TPAVRNLAKDLGID 198
Cdd:TIGR01348 182 TGDLILTLSVAGStpatapapasaqpaAQSPAATQPEPAAAPAAAKAQAPAPQQAGTqnpakvdhaAPAVRRLAREFGVD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 199 INVITGTGKDGRVLKEDVLRFSDQKGFVTDSvSSEHAVIGGDSVSTKASSNFED----KTVPLRGFSRAMVKTMTMA-TS 273
Cdd:TIGR01348 262 LSAVKGTGIKGRILREDVQRFVKEPSVRAQA-AAASAAGGAPGALPWPNVDFSKfgevEEVDMSRIRKISGANLTRNwTM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 274 VPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEH 353
Cdd:TIGR01348 341 IPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPN 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 354 GLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKF 433
Cdd:TIGR01348 421 GLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW 500
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 75186155 434 SKEGTVyPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLML 480
Cdd:TIGR01348 501 NGKEFE-PRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
76-480 |
9.90e-57 |
|
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: 193.41 E-value: 9.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 76 IDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQ 155
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 156 DSLLTTDSSEI----VTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGfvtdsvS 231
Cdd:TIGR01347 81 TAAPPAKSGEEkeetPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPA------S 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 232 SEHAViggdSVSTKASSNFEDKTVPLRGFSRAMVK----------TMTMATSvphFHfveEINCDSLVELK-----QFFK 296
Cdd:TIGR01347 155 AQPPA----AAAAAAAPAAATRPEERVKMTRLRQRiaerlkeaqnSTAMLTT---FN---EVDMSAVMELRkrykeEFEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 297 ENNtdstIKHTFLPTLIKSLSMALTKYPFVNSCFNAEslEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 376
Cdd:TIGR01347 225 KHG----VKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 377 RLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPkFSKEGTVYPASIMMVNIAADHRVL 456
Cdd:TIGR01347 299 DLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDHRLI 377
|
410 420
....*....|....*....|....
gi 75186155 457 DGATVARFCCQWKEYVEKPELLML 480
Cdd:TIGR01347 378 DGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
92-480 |
3.42e-56 |
|
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: 193.09 E-value: 3.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 92 LLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPG-DIIKVGeTLVRLAVEDSQD-----SLLTTDSSE 165
Cdd:TIGR01349 16 LAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVN-KPIAVLVEEKEDvadafKNYKLESSA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 166 IV------TLGGSKQGTENLLGA-----------------------LSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDV 216
Cdd:TIGR01349 95 SPapkpseIAPTAPPSAPKPSPApqkqspepsspaplsdkesgdriFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 217 LRFSDQKGFVTDSVSSEHAVIGGDSVSTKASSNFEDktVPLRGFSRAMVKTMTMA-TSVPHFHFVEEINCDSLVELKQFF 295
Cdd:TIGR01349 175 ESFVPQSPASANQQAAATTPATYPAAAPVSTGSYED--VPLSNIRKIIAKRLLESkQTIPHYYVSIECNVDKLLALRKEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 296 KENNTDsTIKHTFLPTLIKSLSMALTKYPFVNSCFNAEsleIILKGSH-NIGVAMATEHGLVVPNIKNVQSLSLLEITKE 374
Cdd:TIGR01349 253 NAMASE-VYKLSVNDFIIKASALALREVPEANSSWTDN---FIRRYKNvDISVAVATPDGLITPIVRNADAKGLSTISNE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 375 LSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEK--VPKFSKEGTVYPASIMMVNIAAD 452
Cdd:TIGR01349 329 IKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDvaVVDNDEEKGFAVASIMSVTLSCD 408
|
410 420
....*....|....*....|....*...
gi 75186155 453 HRVLDGATVARFCCQWKEYVEKPELLML 480
Cdd:TIGR01349 409 HRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
67-480 |
1.77e-53 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 185.04 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 67 MATDsnsglIDVPlaQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETL 146
Cdd:PRK05704 1 MMVE-----IKVP--TLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 147 VRLAVEDSQDSLLTTDSSEIVTLGGSKQGTENLLGALS----TPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQ 222
Cdd:PRK05704 74 GRIDEGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSndalSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 223 KGfvtdSVSSEHAVIGGDSVSTKASSNFEdKTVP---LRG-FSRAMVK---TMTMATSvphFHfveEINCDSLVELK--- 292
Cdd:PRK05704 154 AA----AAPAAPAAAAPAAAPAPLGARPE-ERVPmtrLRKtIAERLLEaqnTTAMLTT---FN---EVDMTPVMDLRkqy 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 293 --QFFKENNtdstIKHTFLPTLIKSLSMALTKYPFVNscfnAE--SLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSL 368
Cdd:PRK05704 223 kdAFEKKHG----VKLGFMSFFVKAVVEALKRYPEVN----ASidGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 369 LEITKELSRLQHLAANNKLNPEDVTGGTITLSNigaiGGKFGS----PLLNLPEVAIIALGRIEKVPkFSKEGTVYPASI 444
Cdd:PRK05704 295 AEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFGSlmstPIINPPQSAILGMHKIKERP-VAVNGQIVIRPM 369
|
410 420 430
....*....|....*....|....*....|....*.
gi 75186155 445 MMVNIAADHRVLDGATVARFCCQWKEYVEKPELLML 480
Cdd:PRK05704 370 MYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
76-480 |
4.58e-46 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 165.63 E-value: 4.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 76 IDVPlaQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGEtlvrlavedsq 155
Cdd:PTZ00144 47 IKVP--TMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGA----------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 156 dSLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAkdlgidinvITGTGKdgrvlKEDVLRFSDQKGFVTDSVSSeha 235
Cdd:PTZ00144 114 -PLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAA---------PTPEPP-----AASKPTPPAAAKPPEPAPAA--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 236 vigGDSVSTKASSNFEDKTVPLrgfSRaMVK-----------TMTMATSvphFHfveEINCDSLVELKqffKENNTDSTI 304
Cdd:PTZ00144 176 ---KPPPTPVARADPRETRVPM---SR-MRQriaerlkasqnTCAMLTT---FN---ECDMSALMELR---KEYKDDFQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 305 KHT----FLPTLIKSLSMALTKYPFVNSCFnaESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 380
Cdd:PTZ00144 240 KHGvklgFMSAFVKASTIALKKMPIVNAYI--DGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 381 LAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPkFSKEGTVYPASIMMVNIAADHRVLDGAT 460
Cdd:PTZ00144 318 KARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRP-VVVGNEIVIRPIMYLALTYDHRLIDGRD 396
|
410 420
....*....|....*....|
gi 75186155 461 VARFCCQWKEYVEKPELLML 480
Cdd:PTZ00144 397 AVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
89-480 |
2.51e-45 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 166.18 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 89 ECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPG-DIIKVGEtLVRLAVEDSQD----------- 156
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGE-VIAITVEEEEDigkfkdykpss 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 157 -----------------SLLTTDSSEIVTLGGSKQGTENLLG--ALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVL 217
Cdd:PLN02744 205 saapaapkakpsppppkEEEVEKPASSPEPKASKPSAPPSSGdrIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 218 RFSDQKGFVTDSVSSEHAVIGGDSVSTKASSNFEDKTVplrgfSRAMVKTMTmatsVPHFHFVEEINCDSLVELKQFFKE 297
Cdd:PLN02744 285 DYLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTA-----SRLLQSKQT----IPHYYLTVDTRVDKLMALRSQLNS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 298 NNTDSTIKHTFLPTL-IKSLSMALTKYPFVNSCFNAEsleiILKGSHN--IGVAMATEHGLVVPNIKNVQSLSLLEITKE 374
Cdd:PLN02744 356 LQEASGGKKISVNDLvIKAAALALRKVPQCNSSWTDD----YIRQYHNvnINVAVQTENGLYVPVVKDADKKGLSTIAEE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 375 LSRLQHLAANNKLNPEDVTGGTITLSNigaIGGKFG----SPLLNLPEVAIIALGRIEK--VPKfSKEGTVYPASIMMVN 448
Cdd:PLN02744 432 VKQLAQKARENSLKPEDYEGGTFTVSN---LGGPFGikqfCAIINPPQSAILAVGSAEKrvIPG-SGPDQYNFASFMSVT 507
|
410 420 430
....*....|....*....|....*....|..
gi 75186155 449 IAADHRVLDGATVARFCCQWKEYVEKPELLML 480
Cdd:PLN02744 508 LSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
184-475 |
8.08e-31 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 121.94 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 184 STPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGF----VTDSVSSEHAV----------------------- 236
Cdd:PRK14843 8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVrispLAKRIALEHNIawqeiqgtghrgkimkkdvlall 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 237 ---IGGDSVSTKASSNF----EDKT--------VPLRGFSRAMVKTMTMA-TSVPHFHFVEEINCDSLVELKQFFKENNT 300
Cdd:PRK14843 88 penIENDSIKSPAQIEKveevPDNVtpygeierIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKVLEPIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 301 DSTIKHTFLPTLIkSLSM--ALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRL 378
Cdd:PRK14843 168 EATGKKTTVTDLL-SLAVvkTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 379 QHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGR-IEKVPKFSKEGTVYPasIMMVNIAADHRVLD 457
Cdd:PRK14843 247 IGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSStIEKPVVVNGEIVIRP--IMSLGLTIDHRVVD 324
|
330
....*....|....*...
gi 75186155 458 GATVARFCCQWKEYVEKP 475
Cdd:PRK14843 325 GMAGAKFMKDLKELIETP 342
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
71-482 |
2.15e-24 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 105.61 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 71 SNSG-LIDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:PLN02226 86 SESGdTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 150 AVEDSQDSLLTTdsseivtlggSKQGTENLLGALSTPAvrnlakdlgidinvitgtgkdgrvlkEDvlrfsDQKGFVTDS 229
Cdd:PLN02226 166 SKSEDAASQVTP----------SQKIPETTDPKPSPPA--------------------------ED-----KQKPKVESA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 230 VSSEHAVIGGDSVSTKASSNF-------EDKTVPL-RGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTD 301
Cdd:PLN02226 205 PVAEKPKAPSSPPPPKQSAKEpqlppkeRERRVPMtRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 302 S-TIKHTFLPTLIKSLSMALTKYPFVNSCFNAEslEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 380
Cdd:PLN02226 285 KhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 381 LAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKeGTVYPASIMMVNIAADHRVLDGAT 460
Cdd:PLN02226 363 KANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVG-GSVVPRPMMYVALTYDHRLIDGRE 441
|
410 420
....*....|....*....|..
gi 75186155 461 VARFCCQWKEYVEKPELLMLQM 482
Cdd:PLN02226 442 AVYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
76-149 |
2.28e-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: 95.93 E-value: 2.28e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75186155 76 IDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
76-150 |
4.02e-22 |
|
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: 89.74 E-value: 4.02e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75186155 76 IDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLA 150
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
77-149 |
1.42e-16 |
|
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: 74.17 E-value: 1.42e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75186155 77 DVPLAQTGEGIAECELlKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:pfam00364 2 EIKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
183-217 |
5.44e-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: 5.44e-14
10 20 30
....*....|....*....|....*....|....*
gi 75186155 183 LSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVL 217
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
241-464 |
4.50e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 62.22 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 241 SVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVE----LKQFFKENntdSTIKHTFLPTLIKSL 316
Cdd:PRK12270 104 AAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAVPAKLLIDnrivINNHLKRT---RGGKVSFTHLIGYAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 317 SMALTKYPFVNSCFNaeslEI-----ILKGSH-NIGVA--MATEHG---LVVPNIKNVQSLSLLEITKELSRLQHLAANN 385
Cdd:PRK12270 181 VQALKAFPNMNRHYA----EVdgkptLVTPAHvNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 386 KLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEkvpkfskegtvYPAS----------------IMMVNI 449
Cdd:PRK12270 257 KLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAME-----------YPAEfqgaseerlaelgiskVMTLTS 325
|
250
....*....|....*
gi 75186155 450 AADHRVLDGATVARF 464
Cdd:PRK12270 326 TYDHRIIQGAESGEF 340
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
84-216 |
7.66e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 60.34 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75186155 84 GEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDsllttds 163
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD------- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 75186155 164 SEIvtlggskqgtenllGALSTPAVRNLAKDlGIDINVITGTGKDGRVLKEDV 216
Cdd:PRK14875 84 AEI--------------DAFIAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV 121
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
92-149 |
2.29e-09 |
|
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: 53.57 E-value: 2.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 75186155 92 LLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
86-154 |
1.79e-08 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 56.93 E-value: 1.79e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75186155 86 GIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDS 154
Cdd:PRK11854 11 GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
96-149 |
1.69e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 47.20 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 75186155 96 FVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
77-149 |
4.38e-06 |
|
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: 44.35 E-value: 4.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75186155 77 DVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
94-149 |
5.73e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 38.23 E-value: 5.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 75186155 94 KWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:PRK08225 14 KIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
92-149 |
8.89e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 41.75 E-value: 8.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 75186155 92 LLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
92-149 |
9.50e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.99 E-value: 9.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75186155 92 LLKWFVKEGDSVEEFQPLcevqsdkATIE-------ITSRFKGKVALISHSPGDIIKVGETLVRL 149
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPL-------LTIEamkmettITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
67-121 |
2.74e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 75186155 67 MATDsnsglIDVP-LAQTGEgiaECELLKWFVKEGDSVEEFQPLCEVQSDKATIEI 121
Cdd:PRK11892 1 MAIE-----ILMPaLSPTME---EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEV 48
|
|
| |
