|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
3-427 |
1.44e-165 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 471.20 E-value: 1.44e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 3 VYQFKLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGA 82
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 83 DPAPAPSESRKEQPLAdgaedptpaqeekipvtatgdaTEPARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQRARDLG 162
Cdd:PRK11856 82 AEAAAAAEAAPEAPAP----------------------EPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 163 IDLGEVRTSGD--RVRHADLDAYLLYHGGSASGRSAAPRA--------DETIKVVGLRRKIAENMQEAKRRIPHFALVEQ 232
Cdd:PRK11856 140 VDLSTVKGSGPggRITKEDVEAAAAAAAPAAAAAAAAAAAppaaaaegEERVPLSGMRKAIAKRMVESKREIPHFTLTDE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 233 FDVTALEEARAMMNRdrgSNPKLTLLPFLITAMTKAMADWPMINATYDDDAnvVTRHGAVHMGVATQTDGGLMVPVIRNA 312
Cdd:PRK11856 220 VDVTALLALRKQLKA---IGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 313 QQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVIVDGELEARKV 392
Cdd:PRK11856 295 DKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKV 374
|
410 420 430
....*....|....*....|....*....|....*
gi 1707767650 393 MNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PRK11856 375 MPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-427 |
1.61e-128 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 381.86 E-value: 1.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 2 SVYQFKLPDIGEgIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDG 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 82 ADPAPAPsesrkeqpladgAEDPTPAQEEKIPVtatgdatePARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQRARDL 161
Cdd:PRK11855 197 AAPAAAA------------APAAAAPAAAAAAA--------PAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLAREL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 162 GIDLGEVRTSG--DRVRHADLDAYLLY--------------HGGSASGRSAAPRAD-------ETIKVVGLRRKIAENMQ 218
Cdd:PRK11855 257 GVDLSQVKGTGkkGRITKEDVQAFVKGamsaaaaaaaaaaaAGGGGLGLLPWPKVDfskfgeiETKPLSRIKKISAANLH 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 219 EAKRRIPHFALVEQFDVTALEEARAMMNRD-RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRHGAVHMGVA 297
Cdd:PRK11855 337 RSWVTIPHVTQFDEADITDLEALRKQLKKEaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 298 TQTDGGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQ 377
Cdd:PRK11855 417 VDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQ 496
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1707767650 378 EIPVIVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PRK11855 497 MKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
217-427 |
2.51e-91 |
|
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: 274.81 E-value: 2.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 217 MQEAKRRIPHFALVEQFDVTALEEARAMMNRDR-GSNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRHGAVHMG 295
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAaDEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 296 VATQTDGGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNK 375
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1707767650 376 LQEIPVIVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-429 |
3.59e-90 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 279.30 E-value: 3.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 6 FKLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGADPA 85
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 86 PAPSesrkeqpladgaedptpaqeeKIPVTATGDATEPARDPAPQSkaepapapstpaTQGKVLASPAVRQRARDLGIDL 165
Cdd:PLN02528 81 RSDS---------------------LLLPTDSSNIVSLAESDERGS------------NLSGVLSTPAVRHLAKQYGIDL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 166 GEVRTSGD--RVRHADLDAYLLYHGG----------------SASGRSAAPRA----DETIKVVGLRRKIAENMQEAKrR 223
Cdd:PLN02528 128 NDILGTGKdgRVLKEDVLKYAAQKGVvkdsssaeeatiaeqeEFSTSVSTPTEqsyeDKTIPLRGFQRAMVKTMTAAA-K 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 224 IPHFALVEQFDVTALEEARAMMNRDRG-SNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRHGAVHMGVATQTDG 302
Cdd:PLN02528 207 VPHFHYVEEINVDALVELKASFQENNTdPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 303 GLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVI 382
Cdd:PLN02528 287 GLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRF 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1707767650 383 VD-GELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLLSH 429
Cdd:PLN02528 367 VDdGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLH 414
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
7-427 |
7.47e-87 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 276.88 E-value: 7.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 7 KLPDIGEGiaEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGADPAP 86
Cdd:PRK11854 210 NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 87 APSESRKEQPLAdgaedptpaqeekipvtatgdATEPARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQRARDLGIDLG 166
Cdd:PRK11854 288 APAKQEAAAPAP---------------------AAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 167 EVRTSG--DRVRHADLDAYL-------------LYHGGSASGRSAAPRAD-------ETIKVVGLRRKIAENMQEAKRRI 224
Cdd:PRK11854 347 KVKGTGrkGRILKEDVQAYVkdavkraeaapaaAAAGGGGPGLLPWPKVDfskfgeiEEVELGRIQKISGANLHRNWVMI 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 225 PHFALVEQFDVTALEEARAMMNRD---RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRHGAVHMGVATQTD 301
Cdd:PRK11854 427 PHVTQFDKADITELEAFRKQQNAEaekRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTP 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 302 GGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPV 381
Cdd:PRK11854 507 NGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPV 586
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1707767650 382 IVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PRK11854 587 WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLV 632
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-427 |
1.59e-81 |
|
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: 260.96 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 2 SVYQFKLPDIGeGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDG 81
Cdd:TIGR01348 115 GVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 82 ADPAPAPsesrkeQPLADGAEDPTPAQEEKipvtatgdatEPARDPAPQSKAEPAPAPSTPATQGKVL-ASPAVRQRARD 160
Cdd:TIGR01348 194 STPATAP------APASAQPAAQSPAATQP----------EPAAAPAAAKAQAPAPQQAGTQNPAKVDhAAPAVRRLARE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 161 LGIDLGEVRTSG--DRVRHADLDAYLLYHGGSASGRSAA-----------PRAD-------ETIKVVGLRRKIAENMQEA 220
Cdd:TIGR01348 258 FGVDLSAVKGTGikGRILREDVQRFVKEPSVRAQAAAASaaggapgalpwPNVDfskfgevEEVDMSRIRKISGANLTRN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 221 KRRIPHFALVEQFDVTALEEARAMMN-RDRGSNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRHGAVHMGVATQ 299
Cdd:TIGR01348 338 WTMIPHVTHFDKADITEMEAFRKQQNaAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 300 TDGGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEI 379
Cdd:TIGR01348 418 TPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGME 497
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1707767650 380 PVIVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:TIGR01348 498 PVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
7-427 |
3.10e-81 |
|
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: 255.81 E-value: 3.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 7 KLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIEtDGADPAP 86
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGNDATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 87 APSEsrkeqpladgaedptpaqeekipvtatgdATEPARDPAPQSKAEPAPapstPATQGKVLASPAVRQRARDLGIDLG 166
Cdd:TIGR01347 83 APPA-----------------------------KSGEEKEETPAASAAAAP----TAAANRPSLSPAARRLAKEHGIDLS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 167 EVRTSG--DRVRHADLDAYLLYHGGSASGRSAA--------PRADETIKVVGLRRKIAENMQEAKRRIPHFALVEQFDVT 236
Cdd:TIGR01347 130 AVPGTGvtGRVTKEDIIKKTEAPASAQPPAAAAaaaapaaaTRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 237 ALEEARAMMNRD--RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDaNVVTrHGAVHMGVATQTDGGLMVPVIRNAQQ 314
Cdd:TIGR01347 210 AVMELRKRYKEEfeKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVY-KDYYDISVAVSTDRGLVVPVVRNADR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 315 LSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVIVDGELEARKVMN 394
Cdd:TIGR01347 288 MSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMY 367
|
410 420 430
....*....|....*....|....*....|...
gi 1707767650 395 LSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:TIGR01347 368 LALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
7-427 |
2.59e-77 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 246.13 E-value: 2.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 7 KLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGADPAP 86
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 87 APsesrkEQPLADGAEDPTPAQEEKIPVTATGDATePARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQrardlgidlg 166
Cdd:PTZ00144 128 AP-----AAAAAAKAEKTTPEKPKAAAPTPEPPAA-SKPTPPAAAKPPEPAPAAKPPPTPVARADPRETR---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 167 eVRTSGDRVRHADldayllyhggsasgrsaapradetikvvglRRKIAENMqeakrriphFALVEQF---DVTALEEARA 243
Cdd:PTZ00144 192 -VPMSRMRQRIAE------------------------------RLKASQNT---------CAMLTTFnecDMSALMELRK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 244 MMNRD--RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDaNVVTRHgAVHMGVATQTDGGLMVPVIRNAQQLSVWQLA 321
Cdd:PTZ00144 232 EYKDDfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD-EIVYRN-YVDISVAVATPTGLVVPVIRNCENKSFAEIE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 322 REIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVIVDGELEARKVMNLSLSCDH 401
Cdd:PTZ00144 310 KELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDH 389
|
410 420
....*....|....*....|....*.
gi 1707767650 402 RVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PTZ00144 390 RLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
7-427 |
1.35e-75 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 241.28 E-value: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 7 KLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGADPAP 86
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 87 APsesrkeqpladgaedptpaqeekipvtatgdatePARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQRARDLGIDLG 166
Cdd:PRK05704 86 AA----------------------------------AAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDAS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 167 EVRTSG--DRVRHADLDAYLLYHGGSASGRSAAP----------RADETIKVVGLRRKIAENMQEAKRRIphfALVEQF- 233
Cdd:PRK05704 132 AVKGTGkgGRVTKEDVLAALAAAAAAPAAPAAAApaaapaplgaRPEERVPMTRLRKTIAERLLEAQNTT---AMLTTFn 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 234 --DVTALEEARA----MMNRDRGSnpKLTLLPFLITAMTKAMADWPMINATYDDDANVVtrHGAVHMGVATQTDGGLMVP 307
Cdd:PRK05704 209 evDMTPVMDLRKqykdAFEKKHGV--KLGFMSFFVKAVVEALKRYPEVNASIDGDDIVY--HNYYDIGIAVGTPRGLVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 308 VIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVIVDGEL 387
Cdd:PRK05704 285 VLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQI 364
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1707767650 388 EARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PRK05704 365 VIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
7-421 |
5.87e-71 |
|
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: 234.14 E-value: 5.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 7 KLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGADPAP 86
Cdd:TIGR02927 130 KMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPAE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 87 APSESRKEQPLADGAEDPTPAQEEKIPVtatgdATEPARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQRARDLGIDLG 166
Cdd:TIGR02927 210 PAEEEAPAPSEAGSEPAPDPAARAPHAA-----PDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 167 EVRTSG--DRVRHADLDAYL-----LYHGGSASGRSAAPRADE----------------TIKVVGLRRKIAENMQEAKRR 223
Cdd:TIGR02927 285 TVKGTGvgGRIRKQDVLAAAkaaeeARAAAAAPAAAAAPAAPAaaakpaepdtaklrgtTQKMNRIRQITADKTIESLQT 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 224 IPHFALVEQFDVTALEEARAMMNRD--RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRHGAVHMGVATQTD 301
Cdd:TIGR02927 365 SAQLTQVHEVDMTRVAALRARAKNDflEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTP 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 302 GGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPV 381
Cdd:TIGR02927 445 RGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPR 524
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1707767650 382 IVDGE-----LEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLE 421
Cdd:TIGR02927 525 VIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-427 |
1.30e-70 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 229.30 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 7 KLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAG-VVKSLAGEVGDQIAIGSVLVEIETDGADPA 85
Cdd:TIGR01349 3 TMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGyLAKILVPEGTKDVPVNKPIAVLVEEKEDVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 86 PApsesRKEQPLADGA-EDPTPAQEEKipvTATGDATEPARDPAPQSKAEPAPAPSTPATQG-KVLASPAVRQRARDLGI 163
Cdd:TIGR01349 83 DA----FKNYKLESSAsPAPKPSEIAP---TAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGdRIFASPLAKKLAKEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 164 DLGEVRTSG--DRVRHADLDAYL----------LYHGGSASGRSAAPRAD---ETIKVVGLRRKIAENMQEAKRRIPHFA 228
Cdd:TIGR01349 156 DLSAVAGSGpnGRIVKKDIESFVpqspasanqqAAATTPATYPAAAPVSTgsyEDVPLSNIRKIIAKRLLESKQTIPHYY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 229 LVEQFDVTALEEARAMMNRDRGSNPKLTLLPFLITAMTKAMADWPMINATYDDdaNVVTRHGAVHMGVATQTDGGLMVPV 308
Cdd:TIGR01349 236 VSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 309 IRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVIVDGE-- 386
Cdd:TIGR01349 314 VRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEek 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1707767650 387 -LEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:TIGR01349 394 gFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
8-427 |
1.79e-58 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 200.08 E-value: 1.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 8 LPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAG-VVKSLAGEVGDQIAIGSVL---VEIETD--- 80
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGyLAKIVKGDGAKEIKVGEVIaitVEEEEDigk 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 81 ---------GADPAPAPSESrkeqpladgaedPTPAQEEKIPvtatgdatEPARDPAPQSKAEPAPapstPATQGKVLAS 151
Cdd:PLN02744 197 fkdykpsssAAPAAPKAKPS------------PPPPKEEEVE--------KPASSPEPKASKPSAP----PSSGDRIFAS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 152 PAVRQRARDLGIDLGEVRTSG--DRVRHADLDAYLLYHGGSA----SGRSAAPRADET-IKVVGLRRKIAENMQEAKRRI 224
Cdd:PLN02744 253 PLARKLAEDNNVPLSSIKGTGpdGRIVKADIEDYLASGGKGAtappSTDSKAPALDYTdIPNTQIRKVTASRLLQSKQTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 225 PHFALVEQFDVTALEEARAMMN--RDRGSNPKLTLLPFLITAMTKAMADWPMINATYDDDanVVTRHGAVHMGVATQTDG 302
Cdd:PLN02744 333 PHYYLTVDTRVDKLMALRSQLNslQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDD--YIRQYHNVNINVAVQTEN 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 303 GLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSL-GPMGGIASTPVIAPPQVATIAVNKLQE--I 379
Cdd:PLN02744 411 GLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKrvI 490
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1707767650 380 PVIVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PLN02744 491 PGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
147-423 |
5.46e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 176.91 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 147 KVLASPAVRQRARDLGIDLGEVRTSG--DRVRHADLDAYLLYHGGSASGRSAAPRADETI-------------------K 205
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGrdGKILAEDVENFIKSLKSAPTPAEAASVSSAQQaaktaapaaappklegkreK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 206 VVGLRRKIAENMQEAKRRIPHFALVEQFDVTALEEARAMMNRD--RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDA 283
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 284 NVVTRHGAVHMGVATQTDGGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVI 363
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 364 APPQVATIAVNKLQEIPVIVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENP 423
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-427 |
5.28e-44 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 159.54 E-value: 5.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 8 LPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDgADPAP- 86
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS-EDAASq 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 87 -APSESRKEQPladgAEDPTPAQEEKipvtatgdaTEPARDPAPQSKAEPAPAPSTPATQgkvlaspavrqrardlgidl 165
Cdd:PLN02226 175 vTPSQKIPETT----DPKPSPPAEDK---------QKPKVESAPVAEKPKAPSSPPPPKQ-------------------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 166 gevrtsgdrvrhadldayllyhggSASGRSAAPRADET-IKVVGLRRKIAENMQEAKRRIPHFALVEQFDVTALEEARAM 244
Cdd:PLN02226 222 ------------------------SAKEPQLPPKERERrVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 245 MNRD--RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDaNVVTRHgAVHMGVATQTDGGLMVPVIRNAQQLSVWQLAR 322
Cdd:PLN02226 278 YKDAfyEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD-DIIYRD-YVDISIAVGTSKGLVVPVIRGADKMNFAEIEK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 323 EIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLQEIPVIVDGELEARKVMNLSLSCDHR 402
Cdd:PLN02226 356 TINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHR 435
|
410 420
....*....|....*....|....*
gi 1707767650 403 VVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PLN02226 436 LIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
151-427 |
2.01e-39 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 144.66 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 151 SPAVRQRARDLGIDLGEVRTSGDR--VRHADLDAYLLYHGGSASGRSAA-------------PRAD-ETIKVVGLRRKIA 214
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRgkIMKKDVLALLPENIENDSIKSPAqiekveevpdnvtPYGEiERIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 215 ENMQEAKRRIPHFALVEQFDVTaleEARAMMNRD-----RGSNPKLTLLPFLITAMTKAMADWPMINATYDDDANVVTRH 289
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMT---EMLALRKKVlepimEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 290 GAVHMGVATQTDGGLMVPVIRNAQQLSVWQLAREIVRLSEAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVA 369
Cdd:PRK14843 209 NYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSA 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1707767650 370 TIAVNKLQEIPVIVDGELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLLENPLRLL 427
Cdd:PRK14843 289 ILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-77 |
5.23e-28 |
|
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: 105.53 E-value: 5.23e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707767650 2 SVYQFKLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEI 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
6.27e-28 |
|
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: 105.18 E-value: 6.27e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707767650 4 YQFKLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEI 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
79-420 |
8.05e-24 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 104.59 E-value: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 79 TDGADPAPAPSESRKEQPLADGAEDPTPAQEekiPVTATGDATEPARDPAPQSKAEPAPAPSTPATQGKVLASPAvrqra 158
Cdd:PRK12270 39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAA---PAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAA----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 159 rdlgidlgevrtsgdrvrhadldayllyhggsasgrsaAPRADETIKVVGLRRKIAENMqEAKRRIPHFALVEQFDVTAL 238
Cdd:PRK12270 111 --------------------------------------AAVEDEVTPLRGAAAAVAKNM-DASLEVPTATSVRAVPAKLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 239 EEARAMMN----RDRGSNPKLT-LLPFlitAMTKAMADWPMINATYD--DDANVVTRHGAVHMGVA---TQTDGG--LMV 306
Cdd:PRK12270 152 IDNRIVINnhlkRTRGGKVSFThLIGY---ALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAidlPKKDGSrqLVV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 307 PVIRNAQQLSV---WQLAREIVRlseAARSGKASREELSGPTFTISSLGPMGGIASTPVIAPPQVATIAVNKLqEIPVIV 383
Cdd:PRK12270 229 PAIKGAETMDFaqfWAAYEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEF 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1707767650 384 DG-------ELEARKVMNLSLSCDHRVVDGWDAASFLQALKGLL 420
Cdd:PRK12270 305 QGaseerlaELGISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-77 |
2.55e-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: 78.80 E-value: 2.55e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707767650 5 QFKLPDIGEGIAEAeIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEI 77
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
7-74 |
1.08e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 59.57 E-value: 1.08e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707767650 7 KLPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVL 74
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
3.75e-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: 52.80 E-value: 3.75e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707767650 20 IVAWHVQVGDRVEEDQQLAdmmtdkaTVE---ME----SPVAGVVKSLAGEVGDQIAIGSVLVEI 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLA-------VLEamkMEnevtAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
23-160 |
1.18e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 56.85 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 23 WHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVV-KSLAGEVGDQIAIGSVLVEIETDGADPAPAPSesrkeqplADGA 101
Cdd:PRK11892 22 WLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLgKILVPEGTEGVKVNTPIAVLLEEGESASDAGA--------APAA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707767650 102 EDPTPAQEEKIPVTATGDATEPARDPAPQSKAEPAPAPSTPAtqGKVLASPAVRQRARD 160
Cdd:PRK11892 94 AAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPA--GTEMVTMTVREALRD 150
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
8-77 |
1.08e-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: 48.98 E-value: 1.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 8 LPDIGEGIAEAEIVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEI 77
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
148-181 |
1.14e-06 |
|
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: 44.60 E-value: 1.14e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1707767650 148 VLASPAVRQRARDLGIDLGEVRTSGD--RVRHADLD 181
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPggRITKEDVE 36
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
24-78 |
5.12e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 44.01 E-value: 5.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1707767650 24 HVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIE 78
Cdd:PRK08225 16 VVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
68-227 |
4.10e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 45.87 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 68 IAIGSVLVEIETDGADPAPAPSESRKEQPladgaeDPTPAqeekiPVTATGDATEPARDPAPQSKAEPAPAPStPATQGK 147
Cdd:PHA03269 26 IPIPELHTSAATQKPDPAPAPHQAASRAP------DPAVA-----PTSAASRKPDLAQAPTPAASEKFDPAPA-PHQAAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 148 VLASPAVR-QRARDLGIDLGEVRTSGDRVRHADLDAyllyhGGSASGRSAAPRAD-ETIKVVGLRRKIAENMQ---EAKR 222
Cdd:PHA03269 94 RAPDPAVApQLAAAPKPDAAEAFTSAAQAHEAPADA-----GTSAASKKPDPAAHtQHSPPPFAYTRSMEHIActhGGIQ 168
|
....*
gi 1707767650 223 RIPHF 227
Cdd:PHA03269 169 FIPYF 173
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-78 |
4.68e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 45.60 E-value: 4.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707767650 20 IVAWHVQVGDRVEEDQQLA-----DMMTdkatvEMESPVAGVVKSLAGEVGDQIAIGSVLVEIE 78
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLvleamKMEN-----EIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
2.19e-04 |
|
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: 41.03 E-value: 2.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707767650 25 VQVGDRVEEDQQLA-----DMMTdkatvEMESPVAGVVKSLAGEVGDQIAIGSVLVEIE 78
Cdd:COG0511 83 VKVGDKVKAGDTLCiieamKMMN-----EIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
45-200 |
3.36e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.91 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 45 ATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETDGADPAPAPSESRKEQPLADGAEDPTPAQEEKIPVT--------- 115
Cdd:PRK07003 419 AATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAfepapraaa 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 116 ---ATGDATEPARDPAPQSKAEPAPAPSTPATQGKVLASPAVRQRARDLG----IDL---GEVRTSGDRVRHADLDAYLL 185
Cdd:PRK07003 499 psaATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGaaaaLDVlrnAGMRVSSDRGARAAAAAKPA 578
|
170
....*....|....*
gi 1707767650 186 yHGGSASGRSAAPRA 200
Cdd:PRK07003 579 -AAPAAAPKPAAPRV 592
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
20-78 |
4.39e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 42.40 E-value: 4.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707767650 20 IVAWHVQVGDRVEEDQQLADMMTDKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIE 78
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
20-77 |
5.66e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 42.37 E-value: 5.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707767650 20 IVAWHVQVGDRVEEDQQLAdmmtdkaTVE---ME----SPVAGVVKSLAGEVGDQIAIGSVLVEI 77
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLL-------TIEamkMEttitAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
20-78 |
7.22e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.05 E-value: 7.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707767650 20 IVAWHVQVGDRVEEDQQLAdmmtdkaTVE---ME----SPVAGVVKSLAGEVGDQIAIGSVLVEIE 78
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLA-------VIEamkMEttitAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
80-157 |
9.06e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707767650 80 DGADPAPAPSESRKEQPLADGAEDPTPAQEEKIPVTATGDATEPARDPAPQSKAEPAP-----APSTPATQGKVLASPAV 154
Cdd:PRK07764 433 PAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPaaapaAPAAPAAPAGADDAATL 512
|
...
gi 1707767650 155 RQR 157
Cdd:PRK07764 513 RER 515
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
81-153 |
3.40e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.97 E-value: 3.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707767650 81 GADPAPAPSESRKEQPLADGAEDPTPAQEEKIPVTATGDATEPARDPAPQSKAEPAPAPSTPATQGKVLASPA 153
Cdd:PRK07764 412 PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAP 484
|
|
| PRK06748 |
PRK06748 |
hypothetical protein; Validated |
25-80 |
9.72e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180678 [Multi-domain] Cd Length: 83 Bit Score: 35.23 E-value: 9.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1707767650 25 VQVGDRVEEDQQLADMMT-DKATVEMESPVAGVVKSLAGEVGDQIAIGSVLVEIETD 80
Cdd:PRK06748 20 VRESSYVYEWEKLALIETiDKQKVEIKVGISGYIESLEVVEGQAIADQKLLITVRDD 76
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