|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-484 |
2.06e-152 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 440.00 E-value: 2.06e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 5 EFPLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDsaagsi 84
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 85 elqAPGDEEPTGHVTDRADARHTAPTEPSAPAPVADAAeapqpaapaaeegggavlvgygtkgghastrrrrparpesaq 164
Cdd:PRK11856 78 ---EEGEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPA------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 165 adaaeaagaaaegapagaeaagqgaRPASVPAASATPVIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDVIRHAQQAS 244
Cdd:PRK11856 113 -------------------------AAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 245 VFRNIETPEW------GEEREERIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKAspqfAGIRVSPLL 318
Cdd:PRK11856 168 PAAAAAAAAAaappaaAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 319 VMAKAVIWAVQRNPSVNSTWTDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEM 398
Cdd:PRK11856 244 FLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEEL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 399 ANGTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKPWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLE 478
Cdd:PRK11856 324 QGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLE 403
|
....*.
gi 2428672812 479 EPALLL 484
Cdd:PRK11856 404 NPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
3-485 |
5.34e-94 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 295.19 E-value: 5.34e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 3 VSEFPLPDVGEgLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAG 82
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 83 SIELQAPGDEEPTghvtdradarhtAPTEPSAPAPVadaaeapqpaapaaeegggavlvgygtkgghastrrrrPARPES 162
Cdd:PRK11855 198 APAAAAAPAAAAP------------AAAAAAAPAPA--------------------------------------PAAAAA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 163 AqadaaeaagaaaegapagaeaagqgarPASVPAASATP---VIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDVIRH 239
Cdd:PRK11855 228 P---------------------------AAAAPAAAAAPgkaPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 240 AQQASV---------------------FRNIETPEWGEEREEriPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTME 298
Cdd:PRK11855 281 VKGAMSaaaaaaaaaaaagggglgllpWPKVDFSKFGEIETK--PLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 299 FVKRLKASPQFAGIRVSPLLVMAKAVIWAVQRNPSVNSTWTD--QEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRE 376
Cdd:PRK11855 359 LRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEdgDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 377 LAQALEQMTLTARDGKTQPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKPWVIDGEVRPAFVTTVGASF 456
Cdd:PRK11855 439 IAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSY 518
|
490 500
....*....|....*....|....*....
gi 2428672812 457 DHRVVDGDVASRFTADIAAVLEEPALLLD 485
Cdd:PRK11855 519 DHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
275-484 |
1.62e-84 |
|
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: 259.40 E-value: 1.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 275 MVKSAFTAPHVSVFSDVNATRTMEFVKRLKASPQFAGIRVSPLLVMAKAVIWAVQRNPSVNSTWTD--QEIVVHHYVNLG 352
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGeeGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 353 IAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVALGA 432
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2428672812 433 IKQKPWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLEEPALLL 484
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
9-485 |
3.21e-71 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 231.65 E-value: 3.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 9 PDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAGSIELQA 88
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 89 PgdeeptghvtdradarhTAPTEPSAPAPVadaaeapqpaapaaeegggavlvgygtkgghastrrrrparpesaqadaa 168
Cdd:PRK05704 88 A-----------------AAAAAAAAAAPA-------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 169 eaagaaaegapagaeaagqgarPASVPAASATPVIAKPP-IRKLAKDLGVDLATVQATGLVGEITRDDVIRHAQQASVFR 247
Cdd:PRK05704 101 ----------------------QAQAAAAAEQSNDALSPaARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 248 NIETPE--------WGEEREERIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKasPQFA---GIRvsp 316
Cdd:PRK05704 159 AAPAAAapaaapapLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYK--DAFEkkhGVK--- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 317 LLVMA---KAVIWAVQRNPSVNSTWTDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKT 393
Cdd:PRK05704 234 LGFMSffvKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 394 QPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKPWVIDGEV--RP----AFvttvgaSFDHRVVDGDVAS 467
Cdd:PRK05704 314 SIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIviRPmmylAL------SYDHRIIDGKEAV 387
|
490
....*....|....*....
gi 2428672812 468 RFTADIAAVLEEPA-LLLD 485
Cdd:PRK05704 388 GFLVTIKELLEDPErLLLD 406
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
9-485 |
5.67e-70 |
|
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: 228.46 E-value: 5.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 9 PDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAgsielqa 88
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGN------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 89 pgdeeptghvtdradarhTAPTEPSAPAPvadaaeapqpaapaaeegggavlvgygtkgghastrrrrPARPEsaqadaa 168
Cdd:TIGR01347 79 ------------------DATAAPPAKSG---------------------------------------EEKEE------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 169 eaagaaaegapagaeaaGQGARPASVPAASATPVIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDVIRH------AQQ 242
Cdd:TIGR01347 95 -----------------TPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKteapasAQP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 243 ASVFRNIETPEWGEEREERIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKAspQFA---GIRVSPLLV 319
Cdd:TIGR01347 158 PAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKE--EFEkkhGVKLGFMSF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 320 MAKAVIWAVQRNPSVNSTWTDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMA 399
Cdd:TIGR01347 236 FVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 400 NGTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKPWVIDG--EVRPafVTTVGASFDHRVVDGDVASRFTADIAAVL 477
Cdd:TIGR01347 316 GGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGqiEIRP--MMYLALSYDHRLIDGKEAVTFLVTIKELL 393
|
....*....
gi 2428672812 478 EEPA-LLLD 485
Cdd:TIGR01347 394 EDPRrLLLD 402
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
9-478 |
1.58e-66 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 225.27 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 9 PDVGegLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDsAAGSIELQA 88
Cdd:PRK11854 212 PDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE-VEGAAPAAA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 89 PGDEEPTghvtdrADARHTAPTEPSAPAPvadaaeapqpaapaaeegggavlvgygtkgghastrrrrPARPESaqadaa 168
Cdd:PRK11854 289 PAKQEAA------APAPAAAKAEAPAAAP---------------------------------------AAKAEG------ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 169 eaagaaaegapagaeaagqgarpASVPAASATPVIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDV-------IRHAQ 241
Cdd:PRK11854 318 -----------------------KSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVqayvkdaVKRAE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 242 QASVFRNIETPEWG------------EEREErIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLK--ASP 307
Cdd:PRK11854 375 AAPAAAAAGGGGPGllpwpkvdfskfGEIEE-VELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNaeAEK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 308 QFAGIRVSPLLVMAKAVIWAVQRNPSVNSTWTD--QEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMT 385
Cdd:PRK11854 454 RKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEdgQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDIS 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 386 LTARDGKTQPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKP-WVIDgEVRPAFVTTVGASFDHRVVDGD 464
Cdd:PRK11854 534 KKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPvWNGK-EFAPRLMLPLSLSYDHRVIDGA 612
|
490
....*....|....
gi 2428672812 465 VASRFTADIAAVLE 478
Cdd:PRK11854 613 DGARFITIINDRLS 626
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-484 |
1.33e-60 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 204.18 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 6 FPLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDsaagsie 85
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIM------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 86 lqapgdeeptghVTDRADARHTAPTEPSAPAPVADAaeapqpaapaaeegggavlvgYGTKGGHASTRRrrparpesaqa 165
Cdd:PLN02528 74 ------------VEDSQHLRSDSLLLPTDSSNIVSL---------------------AESDERGSNLSG----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 166 daaeaagaaaegapagaeaagqgarpasvpaasatpVIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDVIRHAQQASV 245
Cdd:PLN02528 110 ------------------------------------VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 246 FRN-IETPEWGEEREE-----------------RIPVKGVRKAIAAAMVKSAfTAPHVSVFSDVNATRTMEFVKRLKASP 307
Cdd:PLN02528 154 VKDsSSAEEATIAEQEefstsvstpteqsyedkTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVELKASFQENN 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 308 QFAGIRVSPLLVMAKAVIWAVQRNPSVNSTWTD--QEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMT 385
Cdd:PLN02528 233 TDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEetSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQ 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 386 LTARDGKTQPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKP-WVIDGEVRPAFVTTVGASFDHRVVDGD 464
Cdd:PLN02528 313 HLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASIMTVTIGADHRVLDGA 392
|
490 500
....*....|....*....|
gi 2428672812 465 VASRFTADIAAVLEEPALLL 484
Cdd:PLN02528 393 TVARFCNEWKSYVEKPELLM 412
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-484 |
6.55e-59 |
|
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: 203.18 E-value: 6.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 5 EFPLPDVGEGlTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAGSi 84
Cdd:TIGR01348 2 EIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 85 elQAPGDEepTGHVTDRADARHTAPTEPSAPAPVADAAEAPQPAAPAAEEGGG-----AVLVGYGTK-----------GG 148
Cdd:TIGR01348 80 --QAQAEA--KKEAAPAPTAGAPAPAAQAQAAPAAGQSSGVQEVTVPDIGDIEkvtviEVLVKVGDTvsadqslitleSD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 149 HASTRRRRPAR-------------------------PESAQADAAEAAGAAAEGAPAGAEAAGQGARPASVPAASATPVI 203
Cdd:TIGR01348 156 KASMEVPAPASgvvksvkvkvgdsvptgdliltlsvAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 204 -----------AKPPIRKLAKDLGVDLATVQATGLVGEITRDDVIRHAQQASV------------------FRNIETPEW 254
Cdd:TIGR01348 236 agtqnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVraqaaaasaaggapgalpWPNVDFSKF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 255 GEEREEriPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKASPQFAGIRVSPLLVMAKAVIWAVQRNPSV 334
Cdd:TIGR01348 316 GEVEEV--DMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 335 NSTW--TDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMANGTITITNLGSFG 412
Cdd:TIGR01348 394 NASLdlGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIG 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2428672812 413 MDTGTPILNPGEVGIVALGAIKQKPwVIDG-EVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLEEPALLL 484
Cdd:TIGR01348 474 GTAFTPIVNAPEVAILGVSKSGMEP-VWNGkEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
7-484 |
5.49e-56 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 192.20 E-value: 5.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 7 PLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSaagsiel 86
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDT------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 87 qapgDEEPTGHVTDRADARHTAPTEPSAPAPvadaaeapqpaapaaeegggavlvgygtkgghastrrrRPARPESAQAd 166
Cdd:PTZ00144 121 ----GGAPPAAAPAAAAAAKAEKTTPEKPKA--------------------------------------AAPTPEPPAA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 167 aaeaagaaaegapagaeaagqgarPASVPAASATPVIAKPPIRKLAKdlgvdlatvqatglvgEITRDDvirhaqqasvf 246
Cdd:PTZ00144 158 ------------------------SKPTPPAAAKPPEPAPAAKPPPT----------------PVARAD----------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 247 rnietpewgeEREERIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKasPQFAGIR------VSPLLvm 320
Cdd:PTZ00144 187 ----------PRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK--DDFQKKHgvklgfMSAFV-- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 321 aKAVIWAVQRNPSVNSTWTDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMAN 400
Cdd:PTZ00144 253 -KASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 401 GTITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKPWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLEEP 480
Cdd:PTZ00144 332 GTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDP 411
|
....
gi 2428672812 481 ALLL 484
Cdd:PTZ00144 412 ARML 415
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
206-484 |
8.21e-47 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 165.85 E-value: 8.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 206 PPIRKLAKDLGVDLATVQATGLVGEITRDDV---IRHAQQASVFRNIETPEWGEERE---------ERIPVKGVRKAIAA 273
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVlalLPENIENDSIKSPAQIEKVEEVPdnvtpygeiERIPMTPMRKVIAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 274 AMVKSAFTAPHVSVFSDVNATRTMEFVKR-LKASPQFAGIRVSPLLVMAKAVIWAVQRNPSVNSTWTD--QEIVVHHYVN 350
Cdd:PRK14843 133 RMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEdgKTIITHNYVN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 351 LGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVAL 430
Cdd:PRK14843 213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2428672812 431 GAIKQKPWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLEEPALLL 484
Cdd:PRK14843 293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
202-483 |
1.40e-42 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 153.03 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 202 VIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDVIRH----------AQQASVFRNIET-----PEWGEEREE--RIPV 264
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFikslksaptpAEAASVSSAQQAaktaaPAAAPPKLEgkREKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 265 KGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKASPQ-FAGIRVSPLLVMAKAVIWAVQRNPSVNSTWTD--Q 341
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLkTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEatS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 342 EIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMANGTITITNLGSFGMDTGTPILN 421
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2428672812 422 PGEVGIVALGAIKQKPWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLEEPALL 483
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
5-484 |
3.06e-41 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 155.01 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 5 EFPLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGAT-VEVGTPIirvdsaagS 83
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVI--------A 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 84 IELQAPGDEEPTGHVTDRADARHTAPTEPSAPAPVAdaaeapqpaapaaeegggavlvgygtkgghaSTRRRRPARPESA 163
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPK-------------------------------EEEVEKPASSPEP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 164 QADAaeaagaaaegapagaeaagqgarpASVPAASATPVIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDV----IRH 239
Cdd:PLN02744 235 KASK------------------------PSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIedylASG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 240 AQQASVFRNIETPEWGEEREErIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLKASPQFAG---IRVSP 316
Cdd:PLN02744 291 GKGATAPPSTDSKAPALDYTD-IPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGgkkISVND 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 317 LLVMAKAViwAVQRNPSVNSTWTDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPA 396
Cdd:PLN02744 370 LVIKAAAL--ALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 397 EMANGTITITNLGS-FGMDTGTPILNPGEVGIVALGAIKQK--PWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADI 473
Cdd:PLN02744 448 DYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAF 527
|
490
....*....|.
gi 2428672812 474 AAVLEEPALLL 484
Cdd:PLN02744 528 KGYIENPESML 538
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-485 |
3.70e-41 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 153.37 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 3 VSEFPLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAG 82
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 83 SIELQAPGDEEPtghvtdradarHTAPTEPSAPApvadaaeapqpaapaaeegggavlvgygtkgghastRRRRPARPES 162
Cdd:PLN02226 171 AASQVTPSQKIP-----------ETTDPKPSPPA------------------------------------EDKQKPKVES 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 163 AQAdaaeaagaaaegapagaeaagqgarpASVPAASATPviakPPIRKLAKDlgvdlatvqatglvgeitrddvirhaqq 242
Cdd:PLN02226 204 APV--------------------------AEKPKAPSSP----PPPKQSAKE---------------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 243 asvfrnIETPEwgEEREERIPVKGVRKAIAAAMVKSAFTAPHVSVFSDVNATRTMEFVKRLK-ASPQFAGIRVSPLLVMA 321
Cdd:PLN02226 226 ------PQLPP--KERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKdAFYEKHGVKLGLMSGFI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 322 KAVIWAVQRNPSVNSTWTDQEIVVHHYVNLGIAAATPRGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKTQPAEMANG 401
Cdd:PLN02226 298 KAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 402 TITITNLGSFGMDTGTPILNPGEVGIVALGAIKQKPWVIDGEVRPAFVTTVGASFDHRVVDGDVASRFTADIAAVLEEPA 481
Cdd:PLN02226 378 SFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQ 457
|
....*
gi 2428672812 482 -LLLD 485
Cdd:PLN02226 458 rLLLD 462
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
5-77 |
1.75e-27 |
|
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: 104.76 E-value: 1.75e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2428672812 5 EFPLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRV 77
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-77 |
5.37e-26 |
|
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: 100.56 E-value: 5.37e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2428672812 5 EFPLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRV 77
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-77 |
7.26e-19 |
|
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: 80.72 E-value: 7.26e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2428672812 5 EFPLPDVGEGLTEAeIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRV 77
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
250-477 |
7.62e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 77.62 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 250 ETPEWGEEREERIPVKGVRKAIAAAMVKSaFTAPHVSVFSDVNAT-----RTM--EFVKRLKaspqfaGIRVSPLLVMAK 322
Cdd:PRK12270 106 AAPAAAAVEDEVTPLRGAAAAVAKNMDAS-LEVPTATSVRAVPAKllidnRIVinNHLKRTR------GGKVSFTHLIGY 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 323 AVIWAVQRNPSVNSTWTDQE----IVVHHYVNLGIAAATP-----RGLIVPNLKDAQDMSLRELAQALEQMTLTARDGKT 393
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 394 QPAEMANGTITITNLGSFGMDTGTPILNPGEVGIVALGAIkqkpwvidgEVRPAF---------------VTTVGASFDH 458
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM---------EYPAEFqgaseerlaelgiskVMTLTSTYDH 329
|
250
....*....|....*....
gi 2428672812 459 RVVDGDVASRFTADIAAVL 477
Cdd:PRK12270 330 RIIQGAESGEFLRTIHQLL 348
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
1.85e-12 |
|
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: 62.05 E-value: 1.85e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2428672812 20 IVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRV 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-83 |
9.49e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 66.51 E-value: 9.49e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2428672812 8 LPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAGS 83
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS 82
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
7-77 |
3.68e-11 |
|
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: 58.99 E-value: 3.68e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2428672812 7 PLPDVGEGLTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRV 77
Cdd:cd06663 3 LIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
1.68e-09 |
|
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: 56.06 E-value: 1.68e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2428672812 25 VAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVD 78
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
202-236 |
1.04e-08 |
|
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: 50.76 E-value: 1.04e-08
10 20 30
....*....|....*....|....*....|....*
gi 2428672812 202 VIAKPPIRKLAKDLGVDLATVQATGLVGEITRDDV 236
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
15-117 |
1.16e-07 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 54.15 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428672812 15 LTEAEIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGAT-VEVGTPIIRV----DSAAGSIELQAP 89
Cdd:PRK11892 14 MEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLleegESASDAGAAPAA 93
|
90 100
....*....|....*....|....*....
gi 2428672812 90 GDEEPTGHVTDRA-DARHTAPTEPSAPAP 117
Cdd:PRK11892 94 AAEAAAAAPAAAAaAAAKKAAPAPAAPAA 122
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-77 |
4.62e-07 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 52.15 E-value: 4.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2428672812 20 IVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRV 77
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
25-79 |
5.47e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 44.23 E-value: 5.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2428672812 25 VAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDS 79
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
9-75 |
1.20e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 45.24 E-value: 1.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2428672812 9 PDVGEGLTEA----EIVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPII 75
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
23-75 |
5.75e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 45.69 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2428672812 23 WK--VAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPII 75
Cdd:PRK14040 536 FKviVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
25-71 |
1.51e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 44.36 E-value: 1.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2428672812 25 VAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVG 71
Cdd:PRK12999 1092 VKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG 1138
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
24-88 |
2.68e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.93 E-value: 2.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2428672812 24 KVAPGDAVRVNQVLVEIEtAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAGSIELQA 88
Cdd:COG0845 2 KVERGDVPETVEATGTVE-ARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQ 65
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
20-78 |
3.08e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 40.09 E-value: 3.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2428672812 20 IVHWKVAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPIIRVD 78
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
25-75 |
4.89e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 37.10 E-value: 4.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2428672812 25 VAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPII 75
Cdd:PRK06549 77 VAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
19-59 |
5.49e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 36.36 E-value: 5.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2428672812 19 EIVHWKVA-PGDAVRVNQVLVEIETAKSLVELPSPFAGTVSE 59
Cdd:cd06848 30 DIVFVELPeVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
25-74 |
5.61e-03 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 38.67 E-value: 5.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2428672812 25 VAPGDAVRVNQVLVEIETAKSLVELPSPFAGTVSELLVEEGATVEVGTPI 74
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPL 269
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
47-87 |
8.67e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 34.34 E-value: 8.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2428672812 47 VELPSPFAGTVSELLVEEGATVEVGTPIIRVDSAAGSIELQ 87
Cdd:pfam13533 3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQ 43
|
|
| |
