|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-456 |
9.54e-145 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 419.58 E-value: 9.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 5 MEKLFNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVPa 84
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 85 thqiEEPAGQKAQESTAAAKGAAPTrqptlvgygaavesagrpsrrgrvtAAAVEADPQSESTPKMAAGAVTGAVRARPP 164
Cdd:PRK11856 80 ----GEAEAAAAAEAAPEAPAPEPA-------------------------PAAAAAAAAAPAAAAAPAAPAAAAAKASPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 165 VRKLARDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEfgqghqAADVKPASSNGETRVAVRGVRKATATAM 244
Cdd:PRK11856 131 VRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAA------AAAPPAAAAEGEERVPLSGMRKAIAKRM 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 245 VASAFSAPHVTEFLSVDVTETMELVDRLRAmprlADVKITITSVVAKAVSLLLARHQGLNSRWDEasGEIIEYHYVNLGI 324
Cdd:PRK11856 205 VESKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 325 AAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQV 404
Cdd:PRK11856 279 AVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 405 RKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLIA 456
Cdd:PRK11856 359 VERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
244-455 |
5.46e-85 |
|
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: 259.78 E-value: 5.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 244 MVASAFSAPHVTEFLSVDVTETMELVDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVNLG 323
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 324 IAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQ 403
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 404 VRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
10-455 |
2.63e-65 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 219.36 E-value: 2.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 10 NLPDLGeGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVPATHQIE 89
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPAT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 90 EPAGQKAQESTAAAKGAAPTrqptlvgygaavesagrpsrrgrvtAAAVEADPQSESTPKMAAGAVTGA--VRARPPVRK 167
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPE-------------------------PAAAPAAAKAQAPAPQQAGTQNPAkvDHAAPAVRR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 168 LARDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEFGQGHQAADVKPA---SSNGETR-VAVRGVRKATATA 243
Cdd:TIGR01348 254 LAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNvdfSKFGEVEeVDMSRIRKISGAN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 244 MVASAFSAPHVTEFLSVDVTETMELVDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVNLG 323
Cdd:TIGR01348 334 LTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIG 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 324 IAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQ 403
Cdd:TIGR01348 414 VAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSK 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 404 VRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:TIGR01348 494 SGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
5-80 |
5.61e-24 |
|
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: 94.75 E-value: 5.61e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070139487 5 MEKLFNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISF 80
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
9-77 |
1.02e-22 |
|
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: 91.31 E-value: 1.02e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070139487 9 FNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPI 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-456 |
9.54e-145 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 419.58 E-value: 9.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 5 MEKLFNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVPa 84
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 85 thqiEEPAGQKAQESTAAAKGAAPTrqptlvgygaavesagrpsrrgrvtAAAVEADPQSESTPKMAAGAVTGAVRARPP 164
Cdd:PRK11856 80 ----GEAEAAAAAEAAPEAPAPEPA-------------------------PAAAAAAAAAPAAAAAPAAPAAAAAKASPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 165 VRKLARDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEfgqghqAADVKPASSNGETRVAVRGVRKATATAM 244
Cdd:PRK11856 131 VRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAA------AAAPPAAAAEGEERVPLSGMRKAIAKRM 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 245 VASAFSAPHVTEFLSVDVTETMELVDRLRAmprlADVKITITSVVAKAVSLLLARHQGLNSRWDEasGEIIEYHYVNLGI 324
Cdd:PRK11856 205 VESKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 325 AAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQV 404
Cdd:PRK11856 279 AVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 405 RKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLIA 456
Cdd:PRK11856 359 VERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
9-455 |
1.27e-100 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 311.37 E-value: 1.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 9 FNLPDLGEgLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVpathqi 88
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEV------ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 89 EEPAGQKAQESTAAAKGAAPTRQPtlvgygaavesagrpsrrgrvtAAAVEADPQSESTPKMAAGAVTGAVRARPPVRKL 168
Cdd:PRK11855 195 AAAAPAAAAAPAAAAPAAAAAAAP----------------------APAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 169 ARDSHVDLSTVFGSGEGGLITREDV---VKAVSRSLEESADTAPEFGQGHQAADVKPA---SSNGETR-VAVRGVRKATA 241
Cdd:PRK11855 253 ARELGVDLSQVKGTGKKGRITKEDVqafVKGAMSAAAAAAAAAAAAGGGGLGLLPWPKvdfSKFGEIEtKPLSRIKKISA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 242 TAMVASAFSAPHVTEFLSVDVTETMELVDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVN 321
Cdd:PRK11855 333 ANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFN 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 322 LGIAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAI 401
Cdd:PRK11855 413 IGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGV 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2070139487 402 GQVRKMP-WEyRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:PRK11855 493 GKSQMKPvWD-GKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
244-455 |
5.46e-85 |
|
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: 259.78 E-value: 5.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 244 MVASAFSAPHVTEFLSVDVTETMELVDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVNLG 323
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 324 IAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQ 403
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 404 VRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
10-450 |
5.27e-73 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 241.83 E-value: 5.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 10 NLPDLGegLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVPATHQIE 89
Cdd:PRK11854 210 NVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 90 EPAGQKAQESTAAAKGAAPtrqptlvgygaavesagrpsrrgrvtAAAVEADPQSESTPKMAAGAVtgaVRARPPVRKLA 169
Cdd:PRK11854 288 APAKQEAAAPAPAAAKAEA--------------------------PAAAPAAKAEGKSEFAENDAY---VHATPLVRRLA 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 170 RDSHVDLSTVFGSGEGGLITREDV---VKAVSRSLEESADTAPEFGQGHQAADVKPA--SSNGETR-VAVRGVRKATATA 243
Cdd:PRK11854 339 REFGVNLAKVKGTGRKGRILKEDVqayVKDAVKRAEAAPAAAAAGGGGPGLLPWPKVdfSKFGEIEeVELGRIQKISGAN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 244 MVASAFSAPHVTEFLSVDVTETMEL--VDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVN 321
Cdd:PRK11854 419 LHRNWVMIPHVTQFDKADITELEAFrkQQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVN 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 322 LGIAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAI 401
Cdd:PRK11854 499 IGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGV 578
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2070139487 402 GQVRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRD 450
Cdd:PRK11854 579 SKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
9-455 |
3.11e-67 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 220.75 E-value: 3.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 9 FNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRL-FEPaGAVVNVGNPIISFDVpathq 87
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQInFSP-GDIVKVGETLLKIMV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 88 ieepagqkaqESTAAAKGAAPTrQPTLvgyGAAVESAGRPSRRGRvtaaaveadpqsestpkmaagaVTGAVRARPPVRK 167
Cdd:PLN02528 75 ----------EDSQHLRSDSLL-LPTD---SSNIVSLAESDERGS----------------------NLSGVLSTPAVRH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 168 LARDSHVDLSTVFGSGEGGLITREDVVK-AVSRSLEESADTAPEF--GQGHQAADVKPA---SSNGETRVAVRGVRKATA 241
Cdd:PLN02528 119 LAKQYGIDLNDILGTGKDGRVLKEDVLKyAAQKGVVKDSSSAEEAtiAEQEEFSTSVSTpteQSYEDKTIPLRGFQRAMV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 242 TAMVASAfSAPHVTEFLSVDVTETMELVDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVN 321
Cdd:PLN02528 199 KTMTAAA-KVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 322 LGIAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAI 401
Cdd:PLN02528 278 IGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIAL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2070139487 402 GQVRKMP-WEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:PLN02528 358 GRIQKVPrFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
10-455 |
2.63e-65 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 219.36 E-value: 2.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 10 NLPDLGeGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVPATHQIE 89
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPAT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 90 EPAGQKAQESTAAAKGAAPTrqptlvgygaavesagrpsrrgrvtAAAVEADPQSESTPKMAAGAVTGA--VRARPPVRK 167
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPE-------------------------PAAAPAAAKAQAPAPQQAGTQNPAkvDHAAPAVRR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 168 LARDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEFGQGHQAADVKPA---SSNGETR-VAVRGVRKATATA 243
Cdd:TIGR01348 254 LAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNvdfSKFGEVEeVDMSRIRKISGAN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 244 MVASAFSAPHVTEFLSVDVTETMELVDRLRAMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEYHYVNLG 323
Cdd:TIGR01348 334 LTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIG 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 324 IAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQ 403
Cdd:TIGR01348 414 VAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSK 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 404 VRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:TIGR01348 494 SGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
10-455 |
2.15e-63 |
|
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: 210.36 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 10 NLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIisfdvpatHQIE 89
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVL--------AILE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 90 EPAGQkaqeSTAAAKGAAPTRQPTlvgygaavesagrpsrrgrvTAAAVEADPQSESTPKMAAgavtgavrarPPVRKLA 169
Cdd:TIGR01347 76 EGNDA----TAAPPAKSGEEKEET--------------------PAASAAAAPTAAANRPSLS----------PAARRLA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 170 RDSHVDLSTVFGSGEGGLITREDVVKAvsrsLEESADTAPEFGqgHQAADVKPASSNGETRVAVRGVRKATATAMVASAF 249
Cdd:TIGR01347 122 KEHGIDLSAVPGTGVTGRVTKEDIIKK----TEAPASAQPPAA--AAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 250 SAPHVTEFLSVDVTETMELVDRLR-AMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDeaSGEIIEYHYVNLGIAAAT 328
Cdd:TIGR01347 196 STAMLTTFNEVDMSAVMELRKRYKeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEID--GDDIVYKDYYDISVAVST 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 329 ERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQVRKMP 408
Cdd:TIGR01347 274 DRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2070139487 409 WEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:TIGR01347 354 VAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
11-442 |
1.84e-62 |
|
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: 212.57 E-value: 1.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 11 LPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNpIISFDVPATHQIEE 90
Cdd:TIGR02927 131 MPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGT-VLAIIGDANAAPAE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 91 PAGQKAQESTAAakGAAPTRQPTlvgygaavesagrPSRRGRVTAAAVEADPQSESTPKMAAGAVT---GAVRARPPVRK 167
Cdd:TIGR02927 210 PAEEEAPAPSEA--GSEPAPDPA-------------ARAPHAAPDPPAPAPAPAKTAAPAAAAPVSsgdSGPYVTPLVRK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 168 LARDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEFGQGHQAADVKPASSNGETRVAVRG-------VRKAT 240
Cdd:TIGR02927 275 LAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGttqkmnrIRQIT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 241 ATAMVASAFSAPHVTEFLSVDVTETMELvdRLRAMPRLAD---VKITITSVVAKAVSLLLARHQGLNSRWDEASGEIIEY 317
Cdd:TIGR02927 355 ADKTIESLQTSAQLTQVHEVDMTRVAAL--RARAKNDFLEkngVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYH 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 318 HYVNLGIAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSG 397
Cdd:TIGR02927 433 DVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAA 512
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2070139487 398 ILAIGQVRKMPWEYRDE-----VALRKVMTLSLSFDHRVVDGEQGAKFLS 442
Cdd:TIGR02927 513 ILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLT 562
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
12-455 |
6.42e-59 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 198.52 E-value: 6.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 12 PDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIisfdvpatHQIEEP 91
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL--------GRIDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 92 AGQKAQESTAAAKGAAPTrqptlvgygaavesagrpsrrgrvTAAAVEADPQSESTPKMAAgavtgavrarPPVRKLARD 171
Cdd:PRK05704 80 AAAGAAAAAAAAAAAAAA------------------------APAQAQAAAAAEQSNDALS----------PAARKLAAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 172 SHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEfgqgHQAADVKPASSNGETRVAVRGVRKATATAMVASAFSA 251
Cdd:PRK05704 126 NGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAA----APAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 252 PHVTEFLSVDVTETMELVDRLR-AMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDeasGEIIEYH-YVNLGIAAATE 329
Cdd:PRK05704 202 AMLTTFNEVDMTPVMDLRKQYKdAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASID---GDDIVYHnYYDIGIAVGTP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 330 RGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQVRKMPW 409
Cdd:PRK05704 279 RGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPV 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2070139487 410 EYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:PRK05704 359 AVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
6-455 |
5.87e-58 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 196.44 E-value: 5.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 6 EKLFNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDvpat 85
Cdd:PTZ00144 44 IKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 86 hqieepagqkaqesTAAAKGAAPtrqptlvgygAAVESAGRPSRRGRVTAAAVEADPQSESTPKMAAGAVTGAVRARPPV 165
Cdd:PTZ00144 120 --------------TGGAPPAAA----------PAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 166 RKLArdshvdlstvfgsgegglitredvvKAVSRSLEEsadtapefgqghqaadvkpassngETRVAVRGVRKATATAMV 245
Cdd:PTZ00144 176 KPPP-------------------------TPVARADPR------------------------ETRVPMSRMRQRIAERLK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 246 ASAFSAPHVTEFLSVDVTETMELVDRLR-AMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDeasGEIIEYH-YVNLG 323
Cdd:PTZ00144 207 ASQNTCAMLTTFNECDMSALMELRKEYKdDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYID---GDEIVYRnYVDIS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 324 IAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQ 403
Cdd:PTZ00144 284 VAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHA 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 404 VRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLI 455
Cdd:PTZ00144 364 IKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
156-455 |
4.93e-51 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 176.25 E-value: 4.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 156 TGAVRARPPVRKLARDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEFGQGHQAADVKPASSNGETRVAVRG 235
Cdd:PRK14843 46 TNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEIERIPMTP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 236 VRKATATAMVASAFSAPHVTEFLSVDVTETMELVDRLRAmPRLADV--KITITSVVAKAVSLLLARHQGLNSRWDEASGE 313
Cdd:PRK14843 126 MRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLE-PIMEATgkKTTVTDLLSLAVVKTLMKHPYINASLTEDGKT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 314 IIEYHYVNLGIAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPP 393
Cdd:PRK14843 205 IITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQ 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070139487 394 GQSGILAIGQVRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDP-ALLI 455
Cdd:PRK14843 285 PNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPiSMLI 347
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
11-451 |
6.42e-51 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 180.82 E-value: 6.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 11 LPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAV-VNVGNpIISFDVPATHQIE 89
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGE-VIAITVEEEEDIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 90 EPAGQKAQESTAAAKGAAPTRQPTlvgygAAVESAGRPSRRGRVTAAAVEADPQSEstpkmaagavtGAVRARPPVRKLA 169
Cdd:PLN02744 196 KFKDYKPSSSAAPAAPKAKPSPPP-----PKEEEVEKPASSPEPKASKPSAPPSSG-----------DRIFASPLARKLA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 170 RDSHVDLSTVFGSGEGGLITREDVVKAVSRSLEESADTAPEfgqghqaadVKPASSNGETRVAVRGVRKATATAMVASAF 249
Cdd:PLN02744 260 EDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPST---------DSKAPALDYTDIPNTQIRKVTASRLLQSKQ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 250 SAPHVteFLSVD--VTETMELVDRLRAMPRLADVK-ITITSVVAKAVSLLLARHQGLNSRWdeASGEIIEYHYVNLGIAA 326
Cdd:PLN02744 331 TIPHY--YLTVDtrVDKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSW--TDDYIRQYHNVNINVAV 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 327 ATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNI-GVFGVDSGTPILPPGQSGILAIGQVR 405
Cdd:PLN02744 407 QTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAE 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2070139487 406 K--MPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDP 451
Cdd:PLN02744 487 KrvIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
159-454 |
4.57e-42 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 151.10 E-value: 4.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 159 VRARPPVRKLARDSHVDLSTVFGSGEGGLITREDVVK-----AVSRSLEESADTAPEFGQGHQAADVKPASSNGETRVAV 233
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfikslKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 234 RGVRKATATAMVASAFSAPHVTEFLSVDVTETMELVDRLR-AMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDEASG 312
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 313 EIIEYHYVNLGIAAATERGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILP 392
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 393 PGQSGILAIGQVRKMPWEYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALL 454
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
11-458 |
2.10e-34 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 134.11 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 11 LPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISFDVPATHQIEE 90
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 91 PAGQKAQESTAAaKGAAPTrqptlvgygaavESAGRPsrrgRVTAAAVEADPQSESTPkmaagavtgavrarPPVRKLAR 170
Cdd:PLN02226 176 TPSQKIPETTDP-KPSPPA------------EDKQKP----KVESAPVAEKPKAPSSP--------------PPPKQSAK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 171 DSHVdlstvfgsgegglitredvvkavsrsleesadtapefgqghqaadvkpASSNGETRVAVRGVRKATATAMVASAFS 250
Cdd:PLN02226 225 EPQL------------------------------------------------PPKERERRVPMTRLRKRVATRLKDSQNT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 251 APHVTEFLSVDVTETMELVDRLR-AMPRLADVKITITSVVAKAVSLLLARHQGLNSRWDeaSGEIIEYHYVNLGIAAATE 329
Cdd:PLN02226 257 FALLTTFNEVDMTNLMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVID--GDDIIYRDYVDISIAVGTS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 330 RGLLVPVLKGSQALRLEQVAGEISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQVRKMPW 409
Cdd:PLN02226 335 KGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPM 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2070139487 410 EYRDEVALRKVMTLSLSFDHRVVDGEQGAKFLSELGLILRDPALLIASV 458
Cdd:PLN02226 415 VVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
5-80 |
5.61e-24 |
|
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: 94.75 E-value: 5.61e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070139487 5 MEKLFNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISF 80
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
9-77 |
1.02e-22 |
|
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: 91.31 E-value: 1.02e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070139487 9 FNLPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPI 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
204-441 |
3.94e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 87.64 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 204 SADTAPEFGQGHQAADVKPASSNGETRVAV-RGVRKATATAMVASaFSAPHVTEFLSVDVTetmeLVDRLRAM-----PR 277
Cdd:PRK12270 90 AAAAAAPAAPPAAAAAAAPAAAAVEDEVTPlRGAAAAVAKNMDAS-LEVPTATSVRAVPAK----LLIDNRIVinnhlKR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 278 LADVKITITSVVAKAVSLLLARHQGLNSRWDEASGE--IIEYHYVNLGIAAATE-----RGLLVPVLKGSQALRLEQVAG 350
Cdd:PRK12270 165 TRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGKptLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 351 EISALTAAARSGSITPAQLSGATFTMSNIGVFGVDSGTPILPPGQSGILAIGQVrKMPWEYR-------DEVALRKVMTL 423
Cdd:PRK12270 245 AYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQgaseerlAELGISKVMTL 323
|
250
....*....|....*...
gi 2070139487 424 SLSFDHRVVDGEQGAKFL 441
Cdd:PRK12270 324 TSTYDHRIIQGAESGEFL 341
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
7-78 |
4.47e-14 |
|
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: 66.85 E-value: 4.47e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070139487 7 KLFNLPDLGEGLTESeILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPII 78
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
159-193 |
4.58e-09 |
|
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: 51.53 E-value: 4.58e-09
10 20 30
....*....|....*....|....*....|....*
gi 2070139487 159 VRARPPVRKLARDSHVDLSTVFGSGEGGLITREDV 193
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
11-77 |
2.10e-07 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 52.64 E-value: 2.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070139487 11 LPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPI 77
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
23-80 |
7.35e-07 |
|
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: 46.26 E-value: 7.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070139487 23 ILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISF 80
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
11-80 |
9.90e-07 |
|
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: 46.28 E-value: 9.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 11 LPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPIISF 80
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
11-160 |
2.52e-05 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 46.45 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070139487 11 LPDLGEGLTESEILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAV-VNVGNPIIsfdVPATHQIE 89
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIA---VLLEEGES 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070139487 90 EPAGQKAQESTAAAKGAAPTRQPTLVGYGAAVESAGRPSrrgrvTAAAVEADPQSESTPKMAAGAVTGAVR 160
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAA-----PAAEVAADPDIPAGTEMVTMTVREALR 149
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
29-61 |
7.09e-05 |
|
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: 42.42 E-value: 7.09e-05
10 20 30
....*....|....*....|....*....|...
gi 2070139487 29 AVGENVELNQIIAEVETAKAVVELPSPFSGVVT 61
Cdd:COG0509 46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVV 78
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
30-61 |
1.83e-04 |
|
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: 40.21 E-value: 1.83e-04
10 20 30
....*....|....*....|....*....|..
gi 2070139487 30 VGENVELNQIIAEVETAKAVVELPSPFSGVVT 61
Cdd:cd06848 39 VGTEVKKGDPFGSVESVKAASDLYSPVSGEVV 70
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
22-78 |
7.80e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 37.15 E-value: 7.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070139487 22 EILSWRVAVGENVELNQIIAEVETAKAVVELPSPFSGVVTRLFEPAGAVVNVGNPII 78
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| |
