|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
9-467 |
1.31e-159 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 457.72 E-value: 1.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 9 VREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGG 88
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 89 AAPApaapaqSAEPVAEEEKKPEgrqpvlvgygvatsstkrrprkgpEVAVAQASTAIQtelnghgPAPVASAVPDERPR 168
Cdd:PRK11856 82 AEAA------AAAEAAPEAPAPE------------------------PAPAAAAAAAAA-------PAAAAAPAAPAAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 169 PLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPaasydtARETRVPIKGVRK 248
Cdd:PRK11856 125 AKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAA------EGEERVPLSGMRK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 249 ATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEfaglRVNPLLLIAKALLVAVKRNPDINASWDEAAqeIVVKH 328
Cdd:PRK11856 199 AIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGV----KLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 329 YVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAI 408
Cdd:PRK11856 273 YVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAI 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 971333994 409 LAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLITW 467
Cdd:PRK11856 353 LGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
254-465 |
9.70e-87 |
|
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: 264.41 E-value: 9.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 254 MVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEAAQEIVVKHYVNLG 333
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 334 IAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAILAVGA 413
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 971333994 414 IKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
11-467 |
3.63e-75 |
|
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: 241.18 E-value: 3.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 11 EFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGGAA 90
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 91 PApaapaQSAEPVAEEEKKPegrqpvlvgygvatsstkrrprkgpevavaqastaiqtelnghgPAPVASAVPDERPRPL 170
Cdd:TIGR01347 82 AA-----PPAKSGEEKEETP--------------------------------------------AASAAAAPTAAANRPS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 171 AKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVhaavapPAPAAAPAPVETPAVAAPAPAASYDTARETRVPIKGVRKAT 250
Cdd:TIGR01347 113 LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI------IKKTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRI 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 251 AQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFA-GLRVNPLLLIAKALLVAVKRNPDINASWDeaAQEIVVKHY 329
Cdd:TIGR01347 187 AERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEID--GDDIVYKDY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 330 VNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAIL 409
Cdd:TIGR01347 265 YDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAIL 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 971333994 410 AVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLITW 467
Cdd:TIGR01347 345 GMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
8-83 |
8.83e-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: 102.84 E-value: 8.83e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971333994 8 SVREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
11-83 |
3.01e-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: 100.94 E-value: 3.01e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 11 EFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
9-467 |
1.31e-159 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 457.72 E-value: 1.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 9 VREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGG 88
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 89 AAPApaapaqSAEPVAEEEKKPEgrqpvlvgygvatsstkrrprkgpEVAVAQASTAIQtelnghgPAPVASAVPDERPR 168
Cdd:PRK11856 82 AEAA------AAAEAAPEAPAPE------------------------PAPAAAAAAAAA-------PAAAAAPAAPAAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 169 PLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPaasydtARETRVPIKGVRK 248
Cdd:PRK11856 125 AKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAA------EGEERVPLSGMRK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 249 ATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEfaglRVNPLLLIAKALLVAVKRNPDINASWDEAAqeIVVKH 328
Cdd:PRK11856 199 AIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGV----KLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 329 YVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAI 408
Cdd:PRK11856 273 YVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAI 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 971333994 409 LAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLITW 467
Cdd:PRK11856 353 LGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
7-465 |
1.51e-102 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 316.76 E-value: 1.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 7 ASVREFKMPDVGEgLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVS 86
Cdd:PRK11855 117 GGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 87 GGAAPAPAAPAQSAEPVAEEEKkpegrqpvlvgygvatsstkrrprkgPEVAVAQASTAiqtelnghgPAPVASAVPDER 166
Cdd:PRK11855 196 AAAPAAAAAPAAAAPAAAAAAA--------------------------PAPAPAAAAAP---------AAAAPAAAAAPG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 167 PRPLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVH------AAVAPPAPAAAPAPVETPAVAAPAPAASYDTARETR 240
Cdd:PRK11855 241 KAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQafvkgaMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSKFGEIE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 241 -VPIKGVRKATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFAGLRVNPLLLIAKALLVAVKRNPDINASWDE 319
Cdd:PRK11855 321 tKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 320 AAQEIVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTP 399
Cdd:PRK11855 401 DGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTP 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971333994 400 LLNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PRK11855 481 IINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
254-465 |
9.70e-87 |
|
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: 264.41 E-value: 9.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 254 MVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEAAQEIVVKHYVNLG 333
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 334 IAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAILAVGA 413
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 971333994 414 IKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
7-465 |
9.98e-78 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 254.54 E-value: 9.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 7 ASVREFKMPDVGegLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVS 86
Cdd:PRK11854 204 AGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 87 GGAAPAPAAPAQSAEPVAEEEKKPEgrqpvlvgygvatsstkrrprkgPEVAVAQAstaiqtelnghgpAPVASAVPDER 166
Cdd:PRK11854 282 GAAPAAAPAKQEAAAPAPAAAKAEA-----------------------PAAAPAAK-------------AEGKSEFAEND 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 167 PRPLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPAASYDTA-------RET 239
Cdd:PRK11854 326 AYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGGPGLLPWPKVdfskfgeIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 240 rVPIKGVRKATAQAMVGSAFTAPHVTEFVTVDVTRtmklVEEL-KQDKEFA-----GLRVNPLLLIAKALLVAVKRNPDI 313
Cdd:PRK11854 406 -VELGRIQKISGANLHRNWVMIPHVTQFDKADITE----LEAFrKQQNAEAekrklGVKITPLVFIMKAVAAALEQMPRF 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 314 NASWDEAAQEIVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFG 393
Cdd:PRK11854 481 NSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLG 560
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 394 VDTGTPLLNPGESAILAVGAIKLQPwVHKGK-VKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PRK11854 561 TTHFTPIVNAPEVAILGVSKSAMEP-VWNGKeFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLV 632
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
11-467 |
3.63e-75 |
|
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: 241.18 E-value: 3.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 11 EFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGGAA 90
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 91 PApaapaQSAEPVAEEEKKPegrqpvlvgygvatsstkrrprkgpevavaqastaiqtelnghgPAPVASAVPDERPRPL 170
Cdd:TIGR01347 82 AA-----PPAKSGEEKEETP--------------------------------------------AASAAAAPTAAANRPS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 171 AKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVhaavapPAPAAAPAPVETPAVAAPAPAASYDTARETRVPIKGVRKAT 250
Cdd:TIGR01347 113 LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI------IKKTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRI 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 251 AQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFA-GLRVNPLLLIAKALLVAVKRNPDINASWDeaAQEIVVKHY 329
Cdd:TIGR01347 187 AERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEID--GDDIVYKDY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 330 VNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAIL 409
Cdd:TIGR01347 265 YDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAIL 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 971333994 410 AVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLITW 467
Cdd:TIGR01347 345 GMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
11-465 |
1.78e-72 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 234.34 E-value: 1.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 11 EFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGGAA 90
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 91 PapaapaQSAEPVAEEEKKPEgrqpvlvgygvatsstkrrprkgpevavaqastaiqtelnghgPAPVASAVPDERPRPL 170
Cdd:PRK05704 84 A------AAAAAAAAAAAAAA-------------------------------------------PAQAQAAAAAEQSNDA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 171 AKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVhaavAPPAPAAAPAPVETPAVAAPAPAASYDTARETRVPIKGVRKAT 250
Cdd:PRK05704 115 LSPAARKLAAENGLDASAVKGTGKGGRVTKEDV----LAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 251 AQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKE--------FAGLRVnpllliaKALLVAVKRNPDINASWDeaAQ 322
Cdd:PRK05704 191 AERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEkkhgvklgFMSFFV-------KAVVEALKRYPEVNASID--GD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 323 EIVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLN 402
Cdd:PRK05704 262 DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIIN 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 403 PGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PRK05704 342 PPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-465 |
1.96e-72 |
|
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: 238.24 E-value: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 7 ASVREFKMPDVGeGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVS 86
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 87 GgaapapaapaqSAEPVAEEEKKPEGRQPvlvgygvATSSTKRRPRKGPEVAVAQastaiqtelnghGPAPVASAVPDER 166
Cdd:TIGR01348 193 G-----------STPATAPAPASAQPAAQ-------SPAATQPEPAAAPAAAKAQ------------APAPQQAGTQNPA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 167 PRPLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPA------ASYDTAREtr 240
Cdd:TIGR01348 243 KVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPwpnvdfSKFGEVEE-- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 241 VPIKGVRKATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQDKEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEA 320
Cdd:TIGR01348 321 VDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 321 AQEIVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPL 400
Cdd:TIGR01348 401 GEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPI 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971333994 401 LNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:TIGR01348 481 VNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
12-465 |
7.41e-66 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 217.66 E-value: 7.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 12 FKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGgaap 91
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVED---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 92 apaapaqsaepvaeeekkpegrqpvlvgygvatSSTKRRPRKGPEVAVAQASTAIQTELNGHGPAPVasavpderprpLA 171
Cdd:PLN02528 77 ---------------------------------SQHLRSDSLLLPTDSSNIVSLAESDERGSNLSGV-----------LS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 172 KPPVRKLAKDLGVDLATVIPSGPDGIITRDDV--HAAVAPPAPAAAPAPVETPAVAAPAPAASYDTA----RETRVPIKG 245
Cdd:PLN02528 113 TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkYAAQKGVVKDSSSAEEATIAEQEEFSTSVSTPTeqsyEDKTIPLRG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 246 VRKATAQAMVGSAfTAPHvteFVTVDVTRTMKLVE---ELKQDKEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEAAQ 322
Cdd:PLN02528 193 FQRAMVKTMTAAA-KVPH---FHYVEEINVDALVElkaSFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 323 EIVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLN 402
Cdd:PLN02528 269 EIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLN 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971333994 403 PGESAILAVGAI-KLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PLN02528 349 LPEVAIIALGRIqKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
13-465 |
7.40e-65 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 214.93 E-value: 7.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 13 KMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSGgaapa 92
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 93 paapaqsAEPVAEEEKKPEGRQPvlvgygvatSSTKRRPRKGPEVAVAQASTAiqtelnghgPAPVASAVPDErPRPLAK 172
Cdd:PTZ00144 123 -------APPAAAPAAAAAAKAE---------KTTPEKPKAAAPTPEPPAASK---------PTPPAAAKPPE-PAPAAK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 173 PPvrklakdlgvdlatvipsgPDGIITRDDvhaavappapaaapapvetpavaapapaasydtaRETRVPIKGVRKATAQ 252
Cdd:PTZ00144 177 PP-------------------PTPVARADP----------------------------------RETRVPMSRMRQRIAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 253 AMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEaaQEIVVKHYVN 331
Cdd:PTZ00144 204 RLKASQNTCAMLTTFNECDMSALMELRKEYKDDfQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDG--DEIVYRNYVD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 332 LGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAILAV 411
Cdd:PTZ00144 282 ISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGM 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 971333994 412 GAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PTZ00144 362 HAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
7-460 |
1.96e-61 |
|
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: 210.25 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 7 ASVREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVS 86
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 87 GGaapapaapaqSAEPVAEEEKKPEGRQPVlvgygVATSSTKRRPRKGPEVAVAQASTAIQTELNGhGPAPVASAVPDer 166
Cdd:TIGR02927 204 NA----------APAEPAEEEAPAPSEAGS-----EPAPDPAARAPHAAPDPPAPAPAPAKTAAPA-AAAPVSSGDSG-- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 167 prPLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPAASYDTARETRVPIKG- 245
Cdd:TIGR02927 266 --PYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGt 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 246 ------VRKATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFAGLRVNPLLLIAKALLVAVKRNPDINASWD 318
Cdd:TIGR02927 344 tqkmnrIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYN 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 319 EAAQEIVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGT 398
Cdd:TIGR02927 424 AETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDT 503
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971333994 399 PLLNPGESAILAVGAIKLQPWVHKGK-----VKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQ 460
Cdd:TIGR02927 504 PILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
10-465 |
4.17e-52 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 184.29 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 10 REFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTT-VDVGTAI-ITVDVSG 87
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIaITVEEEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 88 GAAPAPAAPAQSAEPVAEEEKKPEGRQPvlvgygvaTSSTKRRPRKGPEVavaqastaiqtelnghgPAPVASAVPDERP 167
Cdd:PLN02744 193 DIGKFKDYKPSSSAAPAAPKAKPSPPPP--------KEEEVEKPASSPEP-----------------KASKPSAPPSSGD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 168 RPLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVhaavAPPAPAAAPAPVETPAVAAPAPAASYdtareTRVPIKGVR 247
Cdd:PLN02744 248 RIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADI----EDYLASGGKGATAPPSTDSKAPALDY-----TDIPNTQIR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 248 KATAQAMVGSAFTAPHVteFVTVD--VTRTMKLVEELKQDKEFAG---LRVNPLLLIAKALlvAVKRNPDINASW-DEAA 321
Cdd:PLN02744 319 KVTASRLLQSKQTIPHY--YLTVDtrVDKLMALRSQLNSLQEASGgkkISVNDLVIKAAAL--ALRKVPQCNSSWtDDYI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 322 QEIvvkHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNV-GVFGVDTGTPL 400
Cdd:PLN02744 395 RQY---HNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAI 471
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971333994 401 LNPGESAILAVGAI--KLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PLN02744 472 INPPQSAILAVGSAekRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
170-464 |
1.56e-46 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 163.43 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 170 LAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPAASYDTARET-----RVPIK 244
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPklegkREKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 245 GVRKATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEAAQE 323
Cdd:PRK11857 83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 324 IVVKHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNP 403
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971333994 404 GESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRL 464
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
9-465 |
9.09e-42 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 154.53 E-value: 9.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 9 VREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVSgg 88
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 89 aapapaapAQSAEPVAEEEKKPEGRQPvlvgygvaTSSTKRRPRKGPEVAvaqastaiqtelnghgPAPVAsavpdERPR 168
Cdd:PLN02226 169 --------EDAASQVTPSQKIPETTDP--------KPSPPAEDKQKPKVE----------------SAPVA-----EKPK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 169 -PLAKPPVRKLAKDlgvdlatviPSGPDgiitrddvhaavappapaaapapvetpavaapapaasydTARETRVPIKGVR 247
Cdd:PLN02226 212 aPSSPPPPKQSAKE---------PQLPP---------------------------------------KERERRVPMTRLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 248 KATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKQD-KEFAGLRVNPLLLIAKALLVAVKRNPDINASWDeaAQEIVV 326
Cdd:PLN02226 244 KRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVID--GDDIIY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 327 KHYVNLGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGES 406
Cdd:PLN02226 322 RDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 971333994 407 AILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLI 465
Cdd:PLN02226 402 AILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
173-461 |
2.05e-41 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 150.83 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 173 PPVRKLAKDLGVDLATVIPSGPDGIITRDDVHAAVAPPAPAAAPAPVETPAVAAPAPAASYDTARETRVPIKGVRKATAQ 252
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEIERIPMTPMRKVIAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 253 AMVGSAFTAPHVTEFVTVDVTRTMKLVEE-LKQDKEFAGLRVNPLLLIAKALLVAVKRNPDINASWDEAAQEIVVKHYVN 331
Cdd:PRK14843 133 RMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 332 LGIAAATPRGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAAMQGGTVTITNVGVFGVDTGTPLLNPGESAILAV 411
Cdd:PRK14843 213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 971333994 412 GAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQP 461
Cdd:PRK14843 293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
8-83 |
8.83e-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: 102.84 E-value: 8.83e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971333994 8 SVREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
11-83 |
3.01e-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: 100.94 E-value: 3.01e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 11 EFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
11-83 |
5.56e-18 |
|
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: 78.02 E-value: 5.56e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 11 EFKMPDVGEGLTEAeILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
234-444 |
5.11e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 84.17 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 234 DTARETRVPIKGVRKATAQAMVGSaFTAPHVTEFVTVdvtrTMKLVEE--------LKQDKefaGLRVNPLLLIAKALLV 305
Cdd:PRK12270 111 AAVEDEVTPLRGAAAAVAKNMDAS-LEVPTATSVRAV----PAKLLIDnrivinnhLKRTR---GGKVSFTHLIGYALVQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 306 AVKRNPDINASWDEAA--QEIVVKHYVNLGIAAATP-----RGLIVPNVKDAHAKTLPQLAQSLGELVSTAREGKTSPAA 378
Cdd:PRK12270 183 ALKAFPNMNRHYAEVDgkPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADD 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 379 MQGGTVTITNVGVFGVDTGTPLLNPGESAILAVGAIKLqPWVHKGKVKPR-------QVTTLALSFDHRLVDG 444
Cdd:PRK12270 263 FQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEY-PAEFQGASEERlaelgisKVMTLTSTYDHRIIQG 334
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-80 |
1.25e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 69.20 E-value: 1.25e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971333994 8 SVREFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAI 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
169-203 |
1.81e-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: 1.81e-11
10 20 30
....*....|....*....|....*....|....*
gi 971333994 169 PLAKPPVRKLAKDLGVDLATVIPSGPDGIITRDDV 203
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
15-81 |
2.46e-09 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 53.60 E-value: 2.46e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971333994 15 PDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAII 81
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
26-83 |
5.73e-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: 52.42 E-value: 5.73e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 26 ILKWYVQVGDTVTDGQVVCEVETAKaaVELPI--PYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMK--MENEVtaPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
11-115 |
4.01e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 55.31 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971333994 11 EFKMPDVGEGLTEAEILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTT-VDVGTAIITVDVSGGA 89
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLLEEGES 83
|
90 100
....*....|....*....|....*.
gi 971333994 90 APAPAAPAQSAEPVAEEEKKPEGRQP 115
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPAAAAAAA 109
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
30-84 |
1.12e-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: 47.97 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 971333994 30 YVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVD 84
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
15-81 |
2.63e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 47.16 E-value: 2.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971333994 15 PDVGEGLTEA----EILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAII 81
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
26-83 |
4.87e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 49.07 E-value: 4.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 971333994 26 ILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
26-83 |
5.88e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 45.69 E-value: 5.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 971333994 26 ILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITV 83
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
26-86 |
4.25e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 42.79 E-value: 4.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971333994 26 ILKWYVQVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELCFPEGTTVDVGTAIITVDVS 86
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEVS 596
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
32-65 |
5.76e-04 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 39.72 E-value: 5.76e-04
10 20 30
....*....|....*....|....*....|....
gi 971333994 32 QVGDTVTDGQVVCEVETAKAAVELPIPYDGVVRE 65
Cdd:COG0509 46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVE 79
|
|
| |
