|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
3-454 |
1.37e-152 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 439.23 E-value: 1.37e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 3 PQTFLLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIATGVA 82
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 83 SEPdvtvgqSEHGEPEPAPEAEGSVLVGYGTGGPVTSRRRKPAERPVRASVgvvAKPPIRKLARDLGVDLGAVTPTGTAG 162
Cdd:PRK11856 82 AEA------AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAK---ASPAVRKLARELGVDLSTVKGSGPGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 163 EVTRDDVLAHASQAsvfrniatpewpavreeripvAPEVAASAVAPVQATAPSrlagddAHRVETIPVKGVRKATANAMV 242
Cdd:PRK11856 153 RITKEDVEAAAAAA---------------------APAAAAAAAAAAAPPAAA------AEGEERVPLSGMRKAIAKRMV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 243 GSAYSAPHVSVWTDVDATRTMELVKRLKASPdfadVKVSPLLIVARAVIWAVRRTPMVNAAWVDAEegaeIRVRHYVNLG 322
Cdd:PRK11856 206 ESKREIPHFTLTDEVDVTALLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDDDA----IVLKKYVNIG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 323 IAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMGT 402
Cdd:PRK11856 278 IAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGA 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1566295307 403 IRQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:PRK11856 358 IVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-455 |
3.61e-103 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 317.92 E-value: 3.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 2 SPQTFLLPDVGEgLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIatGV 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI--EV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 82 ASEPDVTVGQSEHGEPEPAPEAEGSVLVGYGTGGPVTSrrrkPAErPVRASVGVVAKPPIRKLARDLGVDLGAVTPTGTA 161
Cdd:PRK11855 195 AAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAA----PAA-AAAPGKAPHASPAVRRLARELGVDLSQVKGTGKK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 162 GEVTRDDVLAHASQASvfrniATPEWPAvreeripvAPEVAASAVAPVQATAPsrlAGDDAHR--VETIPVKGVRKATAN 239
Cdd:PRK11855 270 GRITKEDVQAFVKGAM-----SAAAAAA--------AAAAAAGGGGLGLLPWP---KVDFSKFgeIETKPLSRIKKISAA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 240 AMVGSAYSAPHVSVWTDVDATRTMELVKRLKASPDFADVKVSPLLIVARAVIWAVRRTPMVNAAwVDaEEGAEIRVRHYV 319
Cdd:PRK11855 334 NLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNAS-LD-EDGDELTYKKYF 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 320 NLGIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIA 399
Cdd:PRK11855 412 NIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILG 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1566295307 400 MGTIRQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLLD 455
Cdd:PRK11855 492 VGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
241-454 |
3.17e-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: 260.17 E-value: 3.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 241 MVGSAYSAPHVSVWTDVDATRTMELVKRLKASPDFADVKVSPLLIVARAVIWAVRRTPMVNAAWvdAEEGAEIRVRHYVN 320
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASW--DGEEGEIVYKKYVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 321 LGIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAM 400
Cdd:pfam00198 79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1566295307 401 GTIRQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
9-455 |
1.20e-78 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 250.14 E-value: 1.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 9 PDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIATGVASepdvt 88
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 89 vgqsehGEPEPAPEAEgsvlvgygtgGPVTSRRRKPAERPVRASVGVVAKPPIRKLARDLGVDLGAVTPTGTAGEVTRDD 168
Cdd:PRK05704 83 ------GAAAAAAAAA----------AAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 169 VLAHASQAsvfrniatpewpavreeripvapevAASAVAPVQATAPSRLAGDDAHRVETIPVKGVRKATANAMVGSAYSA 248
Cdd:PRK05704 147 VLAALAAA-------------------------AAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 249 PHVSVWTDVDATRTMELVKRLKASpdFA---DVKVSPLLIVARAVIWAVRRTPMVNAAwVDaeeGAEIRVRHYVNLGIAA 325
Cdd:PRK05704 202 AMLTTFNEVDMTPVMDLRKQYKDA--FEkkhGVKLGFMSFFVKAVVEALKRYPEVNAS-ID---GDDIVYHNYYDIGIAV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 326 ATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMGTIRQ 405
Cdd:PRK05704 276 GTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKE 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1566295307 406 KPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPA-LLLD 455
Cdd:PRK05704 356 RPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPErLLLD 406
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
7-455 |
3.56e-77 |
|
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: 246.18 E-value: 3.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 7 LLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIATGvasePD 86
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEG----ND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 87 VTVGQSEHGEPEPAPEaegsvlvgygtggPVTSRRRKPAERPVRASvgvvAKPPIRKLARDLGVDLGAVTPTGTAGEVTR 166
Cdd:TIGR01347 80 ATAAPPAKSGEEKEET-------------PAASAAAAPTAAANRPS----LSPAARRLAKEHGIDLSAVPGTGVTGRVTK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 167 DDVLAHASQasvfrniatpewpavreERIPVAPEVAASAVAPVQATAPsrlagddahrVETIPVKGVRKATANAMVGSAY 246
Cdd:TIGR01347 143 EDIIKKTEA-----------------PASAQPPAAAAAAAAPAAATRP----------EERVKMTRLRQRIAERLKEAQN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 247 SAPHVSVWTDVDATRTMELVKRLKAspDFA---DVKVSPLLIVARAVIWAVRRTPMVNAAWvdaeEGAEIRVRHYVNLGI 323
Cdd:TIGR01347 196 STAMLTTFNEVDMSAVMELRKRYKE--EFEkkhGVKLGFMSFFVKAVVAALKRFPEVNAEI----DGDDIVYKDYYDISV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 324 AAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMGTI 403
Cdd:TIGR01347 270 AVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGI 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 404 RQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPA-LLLD 455
Cdd:TIGR01347 350 KERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRrLLLD 402
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
9-448 |
6.23e-72 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 238.75 E-value: 6.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 9 PDVGegLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIAT-GVASEPDV 87
Cdd:PRK11854 212 PDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVeGAAPAAAP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 88 TVGQSEHGEPEPAPEAEGSVlvgygtggPVTSRRRKPAERPVRASVgVVAKPPIRKLARDLGVDLGAVTPTGTAGEVTRD 167
Cdd:PRK11854 290 AKQEAAAPAPAAAKAEAPAA--------APAAKAEGKSEFAENDAY-VHATPLVRRLAREFGVNLAKVKGTGRKGRILKE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 168 DVLAHASQASvfrniatpewpavreERIPVAPEVAASAVAPVQATAPSRLAGDDAHRVETIPVKGVRKATANAMVGSAYS 247
Cdd:PRK11854 361 DVQAYVKDAV---------------KRAEAAPAAAAAGGGGPGLLPWPKVDFSKFGEIEEVELGRIQKISGANLHRNWVM 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 248 APHVSVWTDVDATRTMELVKRLK--ASPDFADVKVSPLLIVARAVIWAVRRTPMVNAAWvdAEEGAEIRVRHYVNLGIAA 325
Cdd:PRK11854 426 IPHVTQFDKADITELEAFRKQQNaeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSL--SEDGQRLTLKKYVNIGIAV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 326 ATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMGTIRQ 405
Cdd:PRK11854 504 DTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAM 583
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1566295307 406 KPwVVDG-EVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILE 448
Cdd:PRK11854 584 EP-VWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-454 |
1.10e-71 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 232.30 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 6 FLLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIAtgvasep 85
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIM------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 86 dvtVGQSEHGEPEP-APEAEGSVLVGYGTGGPVTSRRRkpaerpvrasvGVVAKPPIRKLARDLGVDLGAVTPTGTAGEV 164
Cdd:PLN02528 74 ---VEDSQHLRSDSlLLPTDSSNIVSLAESDERGSNLS-----------GVLSTPAVRHLAKQYGIDLNDILGTGKDGRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 165 TRDDVLAHASQASVFRNiatpewpavreeriPVAPEVAASAVAPVQATAPSrLAGDDAHRVETIPVKGVRKATANAMVGS 244
Cdd:PLN02528 140 LKEDVLKYAAQKGVVKD--------------SSSAEEATIAEQEEFSTSVS-TPTEQSYEDKTIPLRGFQRAMVKTMTAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 245 AySAPHVSVWTDVDATRTMELVKRLKASPDFADVKVS--PLLIVARAViwAVRRTPMVNAAWVdaEEGAEIRVRHYVNLG 322
Cdd:PLN02528 205 A-KVPHFHYVEEINVDALVELKASFQENNTDPTVKHTflPFLIKSLSM--ALSKYPLLNSCFN--EETSEIRLKGSHNIG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 323 IAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMGT 402
Cdd:PLN02528 280 VAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGR 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 403 IRQKPWVVD-GEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:PLN02528 360 IQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
8-454 |
2.48e-62 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 208.00 E-value: 2.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 8 LPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIATGVASEPDV 87
Cdd:PTZ00144 49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 88 TVGQSEHGEPEPAPEAEgsvlvgygtggpvtsrrrkpaerpvrasvgvvakppirklardlgvDLGAVTPTGtagevtrd 167
Cdd:PTZ00144 129 PAAAAAAKAEKTTPEKP----------------------------------------------KAAAPTPEP-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 168 dvlahasqasvfrnIATPEWPAVREERIPVAPEVAASAVAPVQATAPsrlagddahRVETIPVKGVRKATANAMVGSAYS 247
Cdd:PTZ00144 155 --------------PAASKPTPPAAAKPPEPAPAAKPPPTPVARADP---------RETRVPMSRMRQRIAERLKASQNT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 248 APHVSVWTDVDATRTMELVKRLKasPDFA---DVK---VSPLLivaRAVIWAVRRTPMVNAAWvdaeEGAEIRVRHYVNL 321
Cdd:PTZ00144 212 CAMLTTFNECDMSALMELRKEYK--DDFQkkhGVKlgfMSAFV---KASTIALKKMPIVNAYI----DGDEIVYRNYVDI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 322 GIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMG 401
Cdd:PTZ00144 283 SVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMH 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 402 TIRQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:PTZ00144 363 AIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-454 |
2.81e-61 |
|
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: 205.80 E-value: 2.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 7 LLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEG-QTVEVGTPIITIATGVASEP 85
Cdd:TIGR01349 3 TMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 86 DV----TVGQSEHGEPEPAPEAEGSVlVGYGTGGPVTSRRRKPAERPVRASVG-----VVAKPPIRKLARDLGVDLGAVT 156
Cdd:TIGR01349 83 DAfknyKLESSASPAPKPSEIAPTAP-PSAPKPSPAPQKQSPEPSSPAPLSDKesgdrIFASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 157 PTGTAGEVTRDDVlahasqasvfrniatpewpavrEERIPVAPEVAASAVAPVQATAPSRLAGDDAHRVETIPVKGVRKA 236
Cdd:TIGR01349 162 GSGPNGRIVKKDI----------------------ESFVPQSPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 237 TANAMVGSAYSAPHVSVWTDVDATRTMELVKRLKASPDfADVKVSPLLIVARAVIWAVRRTPMVNAAWVDAEegaeIRVR 316
Cdd:TIGR01349 220 IAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMAS-EVYKLSVNDFIIKASALALREVPEANSSWTDNF----IRRY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 317 HYVNLGIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAG 396
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566295307 397 IIAMGTIRQKPWVVDGEVRPRYVTT---VAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:TIGR01349 375 ILAVGAVEDVAVVDNDEEKGFAVASimsVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
8-454 |
4.77e-61 |
|
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: 207.81 E-value: 4.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 8 LPDVGeGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI-------ATG 80
Cdd:TIGR01348 121 VPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLsvagstpATA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 81 VASEPDVTVGQSEHGEPEPAPEAEGSVLVGygTGGPVTSRRRKPAERPVrasvgvvAKPPIRKLARDLGVDLGAVTPTGT 160
Cdd:TIGR01348 200 PAPASAQPAAQSPAATQPEPAAAPAAAKAQ--APAPQQAGTQNPAKVDH-------AAPAVRRLAREFGVDLSAVKGTGI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 161 AGEVTRDDVLAHASQASVfrniatpewpavreeripVAPEVAASAVAPVQATAPsrLAGDDAHR---VETIPVKGVRKAT 237
Cdd:TIGR01348 271 KGRILREDVQRFVKEPSV------------------RAQAAAASAAGGAPGALP--WPNVDFSKfgeVEEVDMSRIRKIS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 238 ANAMVGSAYSAPHVSVWTDVDATRTMELVKRLKASPDFADVKVSPLLIVARAVIWAVRRTPMVNAAWvdAEEGAEIRVRH 317
Cdd:TIGR01348 331 GANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASL--DLGGEQLILKK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 318 YVNLGIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGI 397
Cdd:TIGR01348 409 YVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566295307 398 IAMGTIRQKPwVVDG-EVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:TIGR01348 489 LGVSKSGMEP-VWNGkEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
135-453 |
5.89e-49 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 169.59 E-value: 5.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 135 VVAKPPIRKLARDLGVDLGAVTPTGTAGEVTRDDVLAHasqasvfrnIATPEWPAVREERIPVAPEVAASAvAPVQATAP 214
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENF---------IKSLKSAPTPAEAASVSSAQQAAK-TAAPAAAP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 215 SRLAGddahRVEtiPVKGVRKATANAMVGSAYSAPHVSVWTDVDATRTMELVKRLKAS-PDFADVKVSPLLIVARAVIWA 293
Cdd:PRK11857 72 PKLEG----KRE--KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 294 VRRTPMVNAAWVDAEEgaEIRVRHYVNLGIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTI 373
Cdd:PRK11857 146 LKEFPIFAAKYDEATS--ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 374 TITNIGVFGMDAGTPIINPGEAGIIAMGTIRQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALL 453
Cdd:PRK11857 224 TITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
137-454 |
6.07e-47 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 165.46 E-value: 6.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 137 AKPPIRKLARDLGVDLGAVTPTGTAGEVTRDDVLAHASQASV-----FRNIATP---EWPAVREERIP-----------V 197
Cdd:PRK14843 8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVrisplAKRIALEhniAWQEIQGTGHRgkimkkdvlalL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 198 APEVAASAVAPVQATAPSRLAGDDA---HRVETIPVKGVRKATANAMVGSAYSAPHVSVWTDVDATRTMELVKR-LKASP 273
Cdd:PRK14843 88 PENIENDSIKSPAQIEKVEEVPDNVtpyGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 274 DFADVKVSPLLIVARAVIWAVRRTPMVNAAWvdAEEGAEIRVRHYVNLGIAAATPRGLLVPNIKDAQSMSMRELARALEK 353
Cdd:PRK14843 168 EATGKKTTVTDLLSLAVVKTLMKHPYINASL--TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 354 LTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMGTIRQKPWVVDGEVRPRYVTTVAGSFDHRVVDG 433
Cdd:PRK14843 246 VIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDG 325
|
330 340
....*....|....*....|.
gi 1566295307 434 DGMSRFIADVASILEEPALLL 454
Cdd:PRK14843 326 MAGAKFMKDLKELIETPISML 346
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
8-454 |
3.53e-45 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 165.03 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 8 LPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEG-QTVEVGTpiiTIATGVASEPD 86
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGE---VIAITVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 87 V---------TVGQSEHGEPEPAPEAEGSVLVGYGTGGPvtsrrRKPAERPVRASVG---VVAKPPIRKLARDLGVDLGA 154
Cdd:PLN02744 194 IgkfkdykpsSSAAPAAPKAKPSPPPPKEEEVEKPASSP-----EPKASKPSAPPSSgdrIFASPLARKLAEDNNVPLSS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 155 VTPTGTAGEVTRDDVLahasqasvfrniatpewpavreeripvapEVAASAVAPVQATAPSRLAGDDAHRVEtIPVKGVR 234
Cdd:PLN02744 269 IKGTGPDGRIVKADIE-----------------------------DYLASGGKGATAPPSTDSKAPALDYTD-IPNTQIR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 235 KATANAMVGSAYSAPHVSVWTDVDATRTMELVKRLKASPDFADVK---VSPLLIVARAViwAVRRTPMVNAAWVDAEega 311
Cdd:PLN02744 319 KVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKkisVNDLVIKAAAL--ALRKVPQCNSSWTDDY--- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 312 eIRVRHYVNLGIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNI-GVFGMDAGTPII 390
Cdd:PLN02744 394 -IRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAII 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566295307 391 NPGEAGIIAMGTIRQK--PWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPALLL 454
Cdd:PLN02744 473 NPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
7-455 |
1.99e-42 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 156.07 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 7 LLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIATGVASEPD 86
Cdd:PLN02226 95 VVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 87 VTVGQS--EHGEPEPAPEAEGsvlvgygtggpvtsrRRKPaerpvrasvgvvakppirklardlgvdlgavtptgtagev 164
Cdd:PLN02226 175 VTPSQKipETTDPKPSPPAED---------------KQKP---------------------------------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 165 trddvlahasqasvfrniatpewpavREERIPVA--PEVAASAVAPVQATAPSRLAGDDAHRveTIPVKGVRKATANAMV 242
Cdd:PLN02226 200 --------------------------KVESAPVAekPKAPSSPPPPKQSAKEPQLPPKERER--RVPMTRLRKRVATRLK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 243 GSAYSAPHVSVWTDVDATRTMELVKRLK-ASPDFADVKVSPLLIVARAVIWAVRRTPMVNAAWvdaeEGAEIRVRHYVNL 321
Cdd:PLN02226 252 DSQNTFALLTTFNEVDMTNLMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVI----DGDDIIYRDYVDI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 322 GIAAATPRGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIGVFGMDAGTPIINPGEAGIIAMG 401
Cdd:PLN02226 328 SIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMH 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1566295307 402 TIRQKPWVVDGEVRPRYVTTVAGSFDHRVVDGDGMSRFIADVASILEEPA-LLLD 455
Cdd:PLN02226 408 SIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQrLLLD 462
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-78 |
2.10e-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: 107.07 E-value: 2.10e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1566295307 2 SPQTFLLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIA 78
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
7.94e-27 |
|
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: 102.48 E-value: 7.94e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1566295307 4 QTFLLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
153-447 |
2.63e-21 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 97.27 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 153 GAVTPTGTAGEVTRDDVLAHASQASVFRNIATPEWPAVREeriPVAPEVAASAVAPVQATAPSRLAGDDAHRVETIPVKG 232
Cdd:PRK12270 46 AAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPK---PAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 233 VRKATANAMVGS-----AYSAPHVSVWTDVDaTRTM--ELVKRLKASpdfadvKVSPLLIVARAVIWAVRRTPMVNAAWv 305
Cdd:PRK12270 123 AAAAVAKNMDASlevptATSVRAVPAKLLID-NRIVinNHLKRTRGG------KVSFTHLIGYALVQALKAFPNMNRHY- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 306 DAEEGAEIRVRH-YVNLGIAAATP-----RGLLVPNIKDAQSMSMRELARALEKLTLTARDGKTTPADQQGGTITITNIG 379
Cdd:PRK12270 195 AEVDGKPTLVTPaHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 380 VFGMDAGTPIINPGEAGIIAMGTIrqkpwvvdgEVRPRY---------------VTTVAGSFDHRVVDGDGMSRFIADVA 444
Cdd:PRK12270 275 GIGTVHSVPRLMKGQGAIIGVGAM---------EYPAEFqgaseerlaelgiskVMTLTSTYDHRIIQGAESGEFLRTIH 345
|
...
gi 1566295307 445 SIL 447
Cdd:PRK12270 346 QLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-77 |
1.26e-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: 79.95 E-value: 1.26e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 5 TFLLPDVGEGLTEAeIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-87 |
1.88e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 68.43 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 4 QTFLLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIATGVAS 83
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS 82
|
....
gi 1566295307 84 EPDV 87
Cdd:PRK14875 83 DAEI 86
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
5-77 |
2.30e-12 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 62.07 E-value: 2.30e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 5 TFLLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
2.51e-12 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 61.66 E-value: 2.51e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566295307 20 IVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
7-106 |
1.70e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 62.63 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566295307 7 LLPDVGEGLTEAEIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEG-QTVEVGTPIITIAT-GVASE 84
Cdd:PRK11892 6 LMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEeGESAS 85
|
90 100
....*....|....*....|..
gi 1566295307 85 PDVTVGQSEHGEPEPAPEAEGS 106
Cdd:PRK11892 86 DAGAAPAAAAEAAAAAPAAAAA 107
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-77 |
2.83e-10 |
|
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: 57.98 E-value: 2.83e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 25 VAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
135-170 |
1.17e-08 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 50.38 E-value: 1.17e-08
10 20 30
....*....|....*....|....*....|....*.
gi 1566295307 135 VVAKPPIRKLARDLGVDLGAVTPTGTAGEVTRDDVL 170
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
25-78 |
1.60e-07 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 53.78 E-value: 1.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1566295307 25 VAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIA 78
Cdd:PRK14040 540 VTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-77 |
5.46e-07 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 51.77 E-value: 5.46e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1566295307 20 IVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
25-77 |
9.76e-07 |
|
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: 51.23 E-value: 9.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 25 VAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:COG1038 1092 VKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
9-77 |
9.97e-07 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 48.32 E-value: 9.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566295307 9 PDVGEGLTEA----EIVNWRVAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITI 77
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
25-71 |
1.30e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 47.83 E-value: 1.30e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1566295307 25 VAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVG 71
Cdd:PRK12999 1092 VKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG 1138
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
25-79 |
1.92e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 40.00 E-value: 1.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1566295307 25 VAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIAT 79
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
25-78 |
4.08e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 40.18 E-value: 4.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1566295307 25 VAPGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEILVPEGQTVEVGTPIITIA 78
Cdd:PRK06549 77 VAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
27-60 |
1.57e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 37.90 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|....
gi 1566295307 27 PGDQVAVNDVLVEIETAKSLVELPSPFDGTVGEI 60
Cdd:cd06848 39 VGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
48-78 |
2.07e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.93 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|.
gi 1566295307 48 ELPSPFDGTVGEILVPEGQTVEVGTPIITIA 78
Cdd:COG0845 133 TIRAPFDGVVGERNVEPGQLVSAGTPLFTIA 163
|
|
| |
