|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-422 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 682.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 1 MAEIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGTA 80
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 81 SAPPAPEKAlqlAEEPKPavpvdraeqPAPQPVAVAQAPGQRPIA-SPAARKMAREKGIDLTQVPTVDPLGRVRKQDVAS 159
Cdd:PRK05704 82 AGAAAAAAA---AAAAAA---------AAPAQAQAAAAAEQSNDAlSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 160 FAAQPAAAPQPAPQaaptSTPAAVPTAEAGKPVIREKMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDK 239
Cdd:PRK05704 150 ALAAAAAAPAAPAA----AAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 240 FFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELA 319
Cdd:PRK05704 226 FEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 320 AKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEErIENRPMMYVALSYDHRIIDGK 399
Cdd:PRK05704 306 KKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ-IVIRPMMYLALSYDHRIIDGK 384
|
410 420
....*....|....*....|...
gi 1493997688 400 EAVGFLKTVKDLIENPEDLLLES 422
Cdd:PRK05704 385 EAVGFLVTIKELLEDPERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-422 |
0e+00 |
|
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: 596.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 2 AEIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGTAS 81
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 82 APPAPEKALQLAEEPKPAvpvdrAEQPAPQpvavaqAPGQRPIASPAARKMAREKGIDLTQVPTVDPLGRVRKQDVASFA 161
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAA-----SAAAAPT------AAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 162 AQPAAAPQPapqaaptSTPAAVPTAEAG-KPVIREKMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDKF 240
Cdd:TIGR01347 150 EAPASAQPP-------AAAAAAAAPAAAtRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 241 FEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELAA 320
Cdd:TIGR01347 223 EKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 321 KARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEErIENRPMMYVALSYDHRIIDGKE 400
Cdd:TIGR01347 303 KARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQ-IEIRPMMYLALSYDHRLIDGKE 381
|
410 420
....*....|....*....|..
gi 1493997688 401 AVGFLKTVKDLIENPEDLLLES 422
Cdd:TIGR01347 382 AVTFLVTIKELLEDPRRLLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
4-421 |
5.94e-169 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 479.95 E-value: 5.94e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 4 IKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGTASAP 83
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 84 PAPEKALQLAEEPKPAVPVDRAEQPAPQPVAvaqapgQRPIASPAARKmarekgidltqvPTVDPlgrvrkqdvasfaaq 163
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAPTPEPPAA------SKPTPPAAAKP------------PEPAP--------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 164 paaapqpapqaapTSTPAAVPTAEAGKPVIREKMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDKFFEE 243
Cdd:PTZ00144 174 -------------AAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 244 HDVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELAAKAR 323
Cdd:PTZ00144 241 HGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 324 SNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEErIENRPMMYVALSYDHRIIDGKEAVG 403
Cdd:PTZ00144 321 NNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE-IVIRPIMYLALTYDHRLIDGRDAVT 399
|
410
....*....|....*...
gi 1493997688 404 FLKTVKDLIENPEDLLLE 421
Cdd:PTZ00144 400 FLKKIKDLIEDPARMLLD 417
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-421 |
7.15e-148 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 426.13 E-value: 7.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 1 MAEIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIG-EGT 79
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEeEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 80 ASAPPAPEKALQLAEEPKPAVPVDRAEQPAPQPVAVAQAPGQRPIASPAARKMAREKGIDLTQVPTVDPLGRVRKQDVAS 159
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 160 FAAQPAAAPQPapqaapTSTPAAVPTAEAGKPVIREKMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDLRKRkkdk 239
Cdd:PRK11856 162 AAAAAAPAAAA------AAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 240 fFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELA 319
Cdd:PRK11856 232 -LKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 320 AKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEErIENRPMMYVALSYDHRIIDGK 399
Cdd:PRK11856 311 EKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE-IVVRKVMPLSLSFDHRVIDGA 389
|
410 420
....*....|....*....|..
gi 1493997688 400 EAVGFLKTVKDLIENPEDLLLE 421
Cdd:PRK11856 390 DAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
3-420 |
2.35e-127 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 378.78 E-value: 2.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAEsITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGTASA 82
Cdd:PRK11855 121 EVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 83 PPAPEKALQLAEEPKPAVPVDRAEQPAPQPVAVAQAP---GQRPIASPAARKMAREKGIDLTQVPTVDPLGRVRKQDVAS 159
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAaapGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 160 FAAQPAAAPQPAPQAAPTSTPAAVPTAEAGK-------PVIREKMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDL 232
Cdd:PRK11855 280 FVKGAMSAAAAAAAAAAAAGGGGLGLLPWPKvdfskfgEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEAL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 233 RKRKKdKFFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEI--QGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAE 310
Cdd:PRK11855 360 RKQLK-KEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLdeDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 311 IERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEErIENRPMMYVALS 390
Cdd:PRK11855 439 IAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKE-FVPRLMLPLSLS 517
|
410 420 430
....*....|....*....|....*....|
gi 1493997688 391 YDHRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:PRK11855 518 YDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-421 |
4.20e-114 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 342.12 E-value: 4.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGT-AS 81
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEdAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 82 APPAPEKALQLAEEPKPAVPVDRAEQPAPQPVAVAQAPgQRPIASPAARKMAREkgidltqvPTVDPLGRVRKqdvasfa 161
Cdd:PLN02226 173 SQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKP-KAPSSPPPPKQSAKE--------PQLPPKERERR------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 162 aqpaaapqpapqaaptstpaaVPtaeagkpvirekMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDKFF 241
Cdd:PLN02226 237 ---------------------VP------------MTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 242 EEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELAAK 321
Cdd:PLN02226 284 EKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 322 ARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEERIEnRPMMYVALSYDHRIIDGKEA 401
Cdd:PLN02226 364 ANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVP-RPMMYVALTYDHRLIDGREA 442
|
410 420
....*....|....*....|
gi 1493997688 402 VGFLKTVKDLIENPEDLLLE 421
Cdd:PLN02226 443 VYFLRRVKDVVEDPQRLLLD 462
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
3-413 |
9.70e-103 |
|
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: 316.57 E-value: 9.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGTASA 82
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 83 PPAPEKALQLAEEPKP------------AVPVDRAEQPAPQPVAVAQAPGQR------PIASPAARKMAREKGIDLTQVP 144
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSepapdpaaraphAAPDPPAPAPAPAKTAAPAAAAPVssgdsgPYVTPLVRKLAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 145 TVDPLGRVRKQDVASFAAQPAAAPQPAPQAAPTSTP----AAVPTAEAGKPVIR---EKMSRRRQTIAKRLLEVTQTTAM 217
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPaapaAAAKPAEPDTAKLRgttQKMNRIRQITADKTIESLQTSAQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 218 LTTFNEIDMSAVIDLRKRKKDKFFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGD--EILLKKYYDIGVAVSTDEGL 295
Cdd:TIGR02927 368 LTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVDTPRGL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 296 VVPVVRDCDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAI- 374
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIk 527
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1493997688 375 DEERIEN---RPMMYVALSYDHRIIDGKEAVGFLKTVKDLIE 413
Cdd:TIGR02927 528 DEDGGESiaiRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-420 |
2.45e-100 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 311.94 E-value: 2.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAesITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGegTASA 82
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE--VEGA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 83 PPAPEKALQLAEEPKPAVPvdRAEQPAPQPVAVAQAPGQR------PIASPAARKMAREKGIDLTQVPTVDPLGRVRKQD 156
Cdd:PRK11854 284 APAAAPAKQEAAAPAPAAA--KAEAPAAAPAAKAEGKSEFaendayVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 157 VASFAAQPAAAPQpapqaaptSTPAAVPTAEAGKPV-------------IRE-KMSRRRQTIAKRLLEVTQTTAMLTTFN 222
Cdd:PRK11854 362 VQAYVKDAVKRAE--------AAPAAAAAGGGGPGLlpwpkvdfskfgeIEEvELGRIQKISGANLHRNWVMIPHVTQFD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 223 EIDMSAVIDLRKRKKDKFF-EEHDVRLGFMSFFVKAAVAALKKYPYVNAEI--QGDEILLKKYYDIGVAVSTDEGLVVPV 299
Cdd:PRK11854 434 KADITELEAFRKQQNAEAEkRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 300 VRDCDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAIDEErI 379
Cdd:PRK11854 514 FKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKE-F 592
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1493997688 380 ENRPMMYVALSYDHRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:PRK11854 593 APRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
208-419 |
1.91e-96 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 287.52 E-value: 1.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 208 LLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDKFFEEHDvRLGFMSFFVKAAVAALKKYPYVNAEIQGD--EILLKKYYDI 285
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 286 GVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMH 365
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1493997688 366 SIKLRPVAIDEErIENRPMMYVALSYDHRIIDGKEAVGFLKTVKDLIENPEDLL 419
Cdd:pfam00198 160 RIRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-420 |
3.40e-90 |
|
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: 279.76 E-value: 3.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKG-DTVAVGQAIAIIGE---- 77
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEeked 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 78 ---------GTASAPPAPEK------ALQLAEEPKPAVPVDRAEQPAPQPVAVAqAPGQRPIASPAARKMAREKGIDLTQ 142
Cdd:TIGR01349 81 vadafknykLESSASPAPKPseiaptAPPSAPKPSPAPQKQSPEPSSPAPLSDK-ESGDRIFASPLAKKLAKEKGIDLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 143 VPTVDPLGRVRKQDVASFAAQPAAAPQPAPQAAPTSTPAAVPTAEAGKPViREKMSRRRQTIAKRLLEVTQTTAMLTTFN 222
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVSTGSYE-DVPLSNIRKIIAKRLLESKQTIPHYYVSI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 223 EIDMSAVIDLRKRKKDKFFEEhdVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRD 302
Cdd:TIGR01349 239 ECNVDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 303 CDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPV--AIDEERIE 380
Cdd:TIGR01349 317 ADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVvdNDEEKGFA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1493997688 381 NRPMMYVALSYDHRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:TIGR01349 397 VASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-420 |
2.26e-82 |
|
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: 262.89 E-value: 2.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAeSITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII-GEGTA- 80
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLsVAGSTp 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 81 SAPPAPEKAL-----QLAEEPKPAVPVDRAEQPAPQPV-AVAQAPGQRPIASPAARKMAREKGIDLTQVPTVDPLGRVRK 154
Cdd:TIGR01348 197 ATAPAPASAQpaaqsPAATQPEPAAAPAAAKAQAPAPQqAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 155 QDVASFAAQPAAAPQPAPQAAPTSTPAAVPTAEAG----KPVIREKMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVI 230
Cdd:TIGR01348 277 EDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNVDfskfGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEME 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 231 DLRKRKKDKFfEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQ--GDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNF 308
Cdd:TIGR01348 357 AFRKQQNAAV-EKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 309 AEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILGMHSIKLRPVAiDEERIENRPMMYVA 388
Cdd:TIGR01348 436 TELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW-NGKEFEPRLMLPLS 514
|
410 420 430
....*....|....*....|....*....|..
gi 1493997688 389 LSYDHRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:TIGR01348 515 LSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
3-420 |
5.42e-74 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 240.91 E-value: 5.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKG-DTVAVGQAIAI------- 74
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAItveeeed 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 75 IGEGTASAPPAPEKALQLAEEPKPAVP-VDRAEQPAPQPVAVAQAP------GQRPIASPAARKMAREKGIDLTQVPTVD 147
Cdd:PLN02744 194 IGKFKDYKPSSSAAPAAPKAKPSPPPPkEEEVEKPASSPEPKASKPsappssGDRIFASPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 148 PLGRVRKQDVASFAAQPAAApqpapqaapTSTPAAVPTAEAGKPVIREKMSRRRQTIAKRLLEVTQTTA--MLTTFNEID 225
Cdd:PLN02744 274 PDGRIVKADIEDYLASGGKG---------ATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPhyYLTVDTRVD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 226 msAVIDLRKRKKDKFFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGDEILLKKYYDIGVAVSTDEGLVVPVVRDCDR 305
Cdd:PLN02744 345 --KLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 306 KNFAEIERDIAELAAKARSNKLSLADLQGGTFTITN-GGVFGSLLSTPLLNGPQVGILGMHSIKLRPV-AIDEERIENRP 383
Cdd:PLN02744 423 KGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRVIpGSGPDQYNFAS 502
|
410 420 430
....*....|....*....|....*....|....*..
gi 1493997688 384 MMYVALSYDHRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:PLN02744 503 FMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
11-420 |
3.66e-65 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 214.20 E-value: 3.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 11 ESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQA-IAIIGEGTasappapeka 89
Cdd:PLN02528 8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETlLKIMVEDS---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 90 lQLAEEPKPAVPVDRAEQpapQPVAVAQAPGQRP---IASPAARKMAREKGIDLTQVPTVDPLGRVRKQDVASFAAQPAA 166
Cdd:PLN02528 78 -QHLRSDSLLLPTDSSNI---VSLAESDERGSNLsgvLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 167 APQPAPQAAptSTPAAVPTAEAGKPVIREKMSRRRqTIA----KRLLEVTQTTAM----LTTFNEIDMSAVIDLrKRKKD 238
Cdd:PLN02528 154 VKDSSSAEE--ATIAEQEEFSTSVSTPTEQSYEDK-TIPlrgfQRAMVKTMTAAAkvphFHYVEEINVDALVEL-KASFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 239 KFFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEIQGD--EILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIA 316
Cdd:PLN02528 230 ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 317 ELAAKARSNKLSLADLQGGTFTITN----GGVFGSllstPLLNGPQVGILGMHSIKLRPVAIDEERIENRPMMYVALSYD 392
Cdd:PLN02528 310 RLQHLAAENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGAD 385
|
410 420
....*....|....*....|....*...
gi 1493997688 393 HRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:PLN02528 386 HRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
124-418 |
3.26e-56 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 187.69 E-value: 3.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 124 IASPAARKMAREKGIDLTQVPTVDPLGRVRKQDVASFAAQPAAAPQ--------PAPQAAPTSTPAAVPTAEAGKpviRE 195
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTpaeaasvsSAQQAAKTAAPAAAPPKLEGK---RE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 196 KMSRRRQTIAKRLLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDKFFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEI--Q 273
Cdd:PRK11857 80 KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 274 GDEILLKKYYDIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPL 353
Cdd:PRK11857 160 TSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 354 LNGPQVGILGMHSIklrpvaIDEERIENR-----PMMYVALSYDHRIIDGKEAVGFLKTVKDLIENPEDL 418
Cdd:PRK11857 240 INYPELAIAGVGAI------IDKAIVKNGqivagKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
126-420 |
3.99e-43 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 154.29 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 126 SPAARKMAREKGIDLTQVPTVDPLGRVRKQDVASFAAQPAAAPQPAPQAAPTSTPAAVPTAEAGKPVIREKMSRRRQTIA 205
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEIERIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 206 KRLLEVTQTTAMLTTFNEIDMSAVIDLRKRKKDKFFEEHDVRLGFMSFFVKAAVAALKKYPYVNAEI--QGDEILLKKYY 283
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 284 DIGVAVSTDEGLVVPVVRDCDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGPQVGILG 363
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1493997688 364 MHSIKLRPVAIDEErIENRPMMYVALSYDHRIIDGKEAVGFLKTVKDLIENPEDLLL 420
Cdd:PRK14843 292 VSSTIEKPVVVNGE-IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-75 |
4.11e-31 |
|
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: 113.65 E-value: 4.11e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
1.33e-29 |
|
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: 109.77 E-value: 1.33e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1493997688 1 MAEIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-75 |
3.58e-20 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 83.80 E-value: 3.58e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493997688 3 EIKVPELAESITEGtIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-123 |
1.38e-19 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 90.36 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 1 MA-EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKG-DTVAVGQAIAII--- 75
Cdd:PRK11892 1 MAiEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLlee 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1493997688 76 GEGTASAPPAPEKALQLAEEPKPAVPVDRAEQPAPQPVAVAQAPGQRP 123
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVA 128
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
56-411 |
1.91e-19 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 91.11 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 56 QQLLANKGDT-VAVGQAIAIIGEGTASAPPAPEKAlQLAEEPKPAVPVDRAEQPAPQPVAVAQAPGQRPIASPAARKMAR 134
Cdd:PRK12270 30 REFFADYGPGsTAAPTAAAAAAAAAASAPAAAPAA-KAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 135 EKGidlTQVPTVDPL----GRVRKQDVASFaaqpaaapqpapqaaptstpaAVPTAeagkpvirekMSRRrqTIAKRLLe 210
Cdd:PRK12270 109 AAA---AVEDEVTPLrgaaAAVAKNMDASL---------------------EVPTA----------TSVR--AVPAKLL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 211 vtqttamlttfneIDMSAVI-DLRKRkkdkffeehdVRLGFMSF---FVKAAVAALKKYPYVN---AEIQGDEILLK-KY 282
Cdd:PRK12270 152 -------------IDNRIVInNHLKR----------TRGGKVSFthlIGYALVQALKAFPNMNrhyAEVDGKPTLVTpAH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 283 YDIGVA--VSTDEG---LVVPVVRDCDRKNFAEIERDIAELAAKARSNKLSLADLQGGTFTITNGGVFGSLLSTPLLNGP 357
Cdd:PRK12270 209 VNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKG 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1493997688 358 QVGILGMHSIKLRP--VAIDEERIEN---RPMMYVALSYDHRIIDGKEAVGFLKTVKDL 411
Cdd:PRK12270 289 QGAIIGVGAMEYPAefQGASEERLAElgiSKVMTLTSTYDHRIIQGAESGEFLRTIHQL 347
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
3-115 |
1.42e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 86.54 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIGEGTASA 82
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD 83
|
90 100 110
....*....|....*....|....*....|...
gi 1493997688 83 PPAPEKALQLAEEPKPAVPVDRAEQPAPQPVAV 115
Cdd:PRK14875 84 AEIDAFIAPFARRFAPEGIDEEDAGPAPRKARI 116
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
3-75 |
5.34e-12 |
|
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: 60.92 E-value: 5.34e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493997688 3 EIKVPELAESITEGTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
16-75 |
1.40e-11 |
|
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: 59.74 E-value: 1.40e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 16 GTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
123-157 |
1.87e-11 |
|
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: 58.47 E-value: 1.87e-11
10 20 30
....*....|....*....|....*....|....*
gi 1493997688 123 PIASPAARKMAREKGIDLTQVPTVDPLGRVRKQDV 157
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
24-76 |
9.07e-07 |
|
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: 47.97 E-value: 9.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1493997688 24 KPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIG 76
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
16-75 |
1.52e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 50.23 E-value: 1.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 16 GTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
16-76 |
6.43e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 43.62 E-value: 6.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1493997688 16 GTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIG 76
Cdd:PRK08225 10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
16-76 |
1.06e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 47.62 E-value: 1.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1493997688 16 GTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIG 76
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
16-76 |
3.25e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 37.92 E-value: 3.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1493997688 16 GTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAIIG 76
Cdd:PRK05641 93 GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIELG 153
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
26-72 |
7.83e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 38.55 E-value: 7.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1493997688 26 GDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAI 72
Cdd:PRK14042 544 GDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
16-75 |
9.15e-03 |
|
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: 38.52 E-value: 9.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997688 16 GTIAQWLKKPGDYVEKGESICELETDKVNVEIMAEESGVLQQLLANKGDTVAVGQAIAII 75
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| |
