|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-466 |
7.59e-162 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 463.49 E-value: 7.59e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 5 MIKEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFEVDD 84
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 85 AGSSNGAGSPTAgagsavgasahgapaasgveavgtpakrepnlvgygavvehsgrptrrarvQAPAAEQATVQAEVPAI 164
Cdd:PRK11856 81 EAEAAAAAEAAP---------------------------------------------------EAPAPEPAPAAAAAAAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 165 PEPVAEPQAEVSGERPRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNFSGTADELAVAPVA------AGQGERET 238
Cdd:PRK11856 110 APAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAaaaappAAAAEGEE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 239 RTPIKGVRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKGNrtfeGFKLTPLTIAAKAVLVALRNNPSLNSRWDE 318
Cdd:PRK11856 190 RVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAI----GVKLTVTDFLIKAVALALKKFPELNASWDD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 319 anQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTP 398
Cdd:PRK11856 266 --DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTP 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2187903916 399 ILNPGEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPAMVMTM 466
Cdd:PRK11856 344 IINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
5-464 |
1.86e-120 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 362.60 E-value: 1.86e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 5 MIKEFRLPDLGEgLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFEVDD 84
Cdd:PRK11855 1 MAIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 85 AGSSNGAGSPTAGAGSA---------VGASAHGAPAASGVE--------------------AVG---------------- 119
Cdd:PRK11855 80 AAAAAAAPAAAAAPAAAaaaapapaaAAPAAAAAAAGGGVVevkvpdigeiteveviewlvKVGdtveedqslitvetdk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 120 ----TPAK----------REPNLVGYGAVV------EHSGRPTRRARVQAPAAEQATVQAEVPA---IPEPVAEPQAEVS 176
Cdd:PRK11855 160 atmeIPSPvagvvkeikvKVGDKVSVGSLLvvievaAAAPAAAAAPAAAAPAAAAAAAPAPAPAaaaAPAAAAPAAAAAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 177 GERPRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNF-----SGTADELAVAPVAAGQ---------------GER 236
Cdd:PRK11855 240 GKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFvkgamSAAAAAAAAAAAAGGGglgllpwpkvdfskfGEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 237 ETRtPIKGVRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKGNRTFEGFKLTPLTIAAKAVLVALRNNPSLNSRW 316
Cdd:PRK11855 320 ETK-PLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 317 DEANQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAG 396
Cdd:PRK11855 399 DEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAF 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2187903916 397 TPILNPGEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPA-MVM 464
Cdd:PRK11855 479 TPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRrMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
253-464 |
4.68e-96 |
|
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: 288.29 E-value: 4.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 253 MVQSAFTAPHVTEFLTVDVTATMELLARLKGNRTFEGFKLTPLTIAAKAVLVALRNNPSLNSRWDEANQEIVQFNYVNLG 332
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 333 IAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTPILNPGEAAIVALGA 412
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2187903916 413 VRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPAMVM 464
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-459 |
7.52e-91 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 288.82 E-value: 7.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 2 TATMIKEFRLPDLGegLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFE 81
Cdd:PRK11854 101 AAAAAKDVHVPDIG--SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 82 VddaGSSNGAGSPTAGAGSAVGASAHGAPAASGVE----------------AVGTPAKREPNLVGY-------------- 131
Cdd:PRK11854 179 V---AGEAPAAAPAAAEAAAPAAAPAAAAGVKDVNvpdiggdevevtevmvKVGDKVEAEQSLITVegdkasmevpapfa 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 132 GAVVE---------HSGRPTRRARVQ--APAAEQATVQAEVPAIPEPVAEPQAE-------------VSGERPRSTPPVR 187
Cdd:PRK11854 256 GTVKEikvnvgdkvKTGSLIMRFEVEgaAPAAAPAKQEAAAPAPAAAKAEAPAAapaakaegksefaENDAYVHATPLVR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 188 KLARDLGIDLELVPGTGPGGLITREDVQNFSGTADELA-VAPVAAG------------------QGERETrTPIKGVRKF 248
Cdd:PRK11854 336 RLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAeAAPAAAAaggggpgllpwpkvdfskFGEIEE-VELGRIQKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 249 TAAAMVQSAFTAPHVTEFLTVDVTATMELlaRLKGNRTFE----GFKLTPLTIAAKAVLVALRNNPSLNSRWDEANQEIV 324
Cdd:PRK11854 415 SGANLHRNWVMIPHVTQFDKADITELEAF--RKQQNAEAEkrklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 325 QFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTPILNPGE 404
Cdd:PRK11854 493 LKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPE 572
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2187903916 405 AAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSD 459
Cdd:PRK11854 573 VAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
5-461 |
2.34e-76 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 244.36 E-value: 2.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 5 MIKEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIvsfevdd 84
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 85 agssnGAGSPTAGAGSAVGASAHGAPAAsgveavgtpakrepnlvgygavvehsgrPTRRARVQAPAAEQATVQAevpai 164
Cdd:PRK05704 74 -----GRIDEGAAAGAAAAAAAAAAAAA----------------------------AAPAQAQAAAAAEQSNDAL----- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 165 pepvaepqaevsgerprsTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNFSGTADELAVAPVAAGQ--------GER 236
Cdd:PRK05704 116 ------------------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPaaapaplgARP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 237 ETRTPIKGVRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKgnRTFE---GFKLTPLTIAAKAVLVALRNNPSLN 313
Cdd:PRK05704 178 EERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYK--DAFEkkhGVKLGFMSFFVKAVVEALKRYPEVN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 314 SRWDeaNQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGI 393
Cdd:PRK05704 256 ASID--GDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGS 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2187903916 394 DAGTPILNPGEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPA 461
Cdd:PRK05704 334 LMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPE 401
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
8-461 |
8.90e-76 |
|
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: 242.72 E-value: 8.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 8 EFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFEvddags 87
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 88 sNGAGSPTAgagsavgasahgAPAASGVEAVGTPAKRepnlvgygavvehsgrptrrarvqapaaeqatvqaevpaipep 167
Cdd:TIGR01347 76 -EGNDATAA------------PPAKSGEEKEETPAAS------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 168 vAEPQAEVSGERPRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNFS---GTADELAVA---PVAAGQGERETRTP 241
Cdd:TIGR01347 100 -AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTeapASAQPPAAAaaaAAPAAATRPEERVK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 242 IKGVRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKgnRTFE---GFKLTPLTIAAKAVLVALRNNPSLNSRWDe 318
Cdd:TIGR01347 179 MTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYK--EEFEkkhGVKLGFMSFFVKAVVAALKRFPEVNAEID- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 319 aNQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTP 398
Cdd:TIGR01347 256 -GDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTP 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2187903916 399 ILNPGEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPA 461
Cdd:TIGR01347 335 IINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPR 397
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-464 |
3.04e-74 |
|
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: 243.24 E-value: 3.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 3 ATMIKEFRLPDLGeGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFEV 82
Cdd:TIGR01348 113 SSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 83 DDAgssngagsptagagsavgasahgAPAASGveavgTPAKREPnlvgygavvehsGRPTRRARVQAPAAEQATVQAEVP 162
Cdd:TIGR01348 192 AGS-----------------------TPATAP-----APASAQP------------AAQSPAATQPEPAAAPAAAKAQAP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 163 AIPEPVAEPQAEVsgerPRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNFSGTADELA-VAPVAAGQ-------- 233
Cdd:TIGR01348 232 APQQAGTQNPAKV----DHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAqAAAASAAGgapgalpw 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 234 --------GEREtRTPIKGVRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKGNRTFEGFKLTPLTIAAKAVLVA 305
Cdd:TIGR01348 308 pnvdfskfGEVE-EVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 306 LRNNPSLNSRWDEANQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISI 385
Cdd:TIGR01348 387 LKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTI 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2187903916 386 TNIGVFGIDAGTPILNPGEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPAMVM 464
Cdd:TIGR01348 467 SSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
8-450 |
5.15e-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: 235.68 E-value: 5.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 8 EFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFevddaGS 87
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAII-----GD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 88 SNGAGSPTAGAGSAvgasahgAPAASGVEAVGTPAKREPNlvgygavvehsgrptrrarvqapAAEQATVQAEVPAIPEP 167
Cdd:TIGR02927 203 ANAAPAEPAEEEAP-------APSEAGSEPAPDPAARAPH-----------------------AAPDPPAPAPAPAKTAA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 168 VAEPQAEVSGER-PRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNFSGTADE------------LAVAPVAAGQG 234
Cdd:TIGR02927 253 PAAAAPVSSGDSgPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEaraaaaapaaaaAPAAPAAAAKP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 235 ERETRTPIKG-------VRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKGN-RTFEGFKLTPLTIAAKAVLVAL 306
Cdd:TIGR02927 333 AEPDTAKLRGttqkmnrIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDfLEKNGVNLTFLPFFVQAVTEAL 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 307 RNNPSLNSRWDEANQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISIT 386
Cdd:TIGR02927 413 KAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTIT 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2187903916 387 NIGVFGIDAGTPILNPGEAAIVALGAVRKAPWVVNDE-----LAVRQVMSLSLSFDHRLVDGEQGSRFL 450
Cdd:TIGR02927 493 NIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFL 561
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
9-449 |
3.06e-68 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 223.83 E-value: 3.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 9 FRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFEVDDagss 88
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVED---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 89 ngagsptagagsavgaSAHGAPAASGVEAVGTpakrepNLVGYGAvvehsgrptrrarvqapaaeqatvqaevpaipepv 168
Cdd:PLN02528 77 ----------------SQHLRSDSLLLPTDSS------NIVSLAE----------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 169 aepqAEVSGERPR---STPPVRKLARDLGIDLELVPGTGPGGLITREDVQNF--------SGTADELAVAPV-------- 229
Cdd:PLN02528 100 ----SDERGSNLSgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYaaqkgvvkDSSSAEEATIAEqeefstsv 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 230 --AAGQGERETRTPIKGVRKFTAAAMVQSAfTAPHVTEFLTVDVTATMELLARLKGNRTFEGFKLTPLTIAAKAVLVALR 307
Cdd:PLN02528 176 stPTEQSYEDKTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 308 NNPSLNSRWDEANQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITN 387
Cdd:PLN02528 255 KYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSN 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2187903916 388 IGVFGIDAGTPILNPGEAAIVALGAVRKAPWVVNDELAV-RQVMSLSLSFDHRLVDGEQGSRF 449
Cdd:PLN02528 335 IGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYpASIMTVTIGADHRVLDGATVARF 397
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
6-461 |
1.28e-65 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 216.86 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 6 IKEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIvsFEVDda 85
Cdd:PTZ00144 44 IKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPL--SEID-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 86 gssngagspTAGAGSAVGASAHGAPAASgveavgtpakrepnlvgygavvehsgrPTRRARVQAPAAEQATVQAEVPAIP 165
Cdd:PTZ00144 120 ---------TGGAPPAAAPAAAAAAKAE---------------------------KTTPEKPKAAAPTPEPPAASKPTPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 166 EPVaepqaevsgeRPRSTPPVRKlardlgidlelvpgtgpgglitredvqnfsgtadelAVAPVAAGQGERETRTPIKGV 245
Cdd:PTZ00144 164 AAA----------KPPEPAPAAK------------------------------------PPPTPVARADPRETRVPMSRM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 246 RKFTAAAMVQSAFTAPHVTEFLTVDVTATMELlaRLKGNRTFE---GFKLTPLTIAAKAVLVALRNNPSLNSRWDEanQE 322
Cdd:PTZ00144 198 RQRIAERLKASQNTCAMLTTFNECDMSALMEL--RKEYKDDFQkkhGVKLGFMSAFVKASTIALKKMPIVNAYIDG--DE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 323 IVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTPILNP 402
Cdd:PTZ00144 274 IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINP 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2187903916 403 GEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPA 461
Cdd:PTZ00144 354 PQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPA 412
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
7-467 |
1.49e-55 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 193.53 E-value: 1.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 7 KEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAA-LHEQPGTVVEVGKpIVSFEVDDA 85
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKiVKGDGAKEIKVGE-VIAITVEEE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 86 GSSNGAGSPTAgagsavgaSAHGAPAASGVEAVGTPAKREpnlvgygavvehsgrptrRARVQAPAAEqatvqaevPAIP 165
Cdd:PLN02744 192 EDIGKFKDYKP--------SSSAAPAAPKAKPSPPPPKEE------------------EVEKPASSPE--------PKAS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 166 EPVAEPQaevSGERPRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNF---SGTADELAVAPVAAGQGERETRTPI 242
Cdd:PLN02744 238 KPSAPPS---SGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYlasGGKGATAPPSTDSKAPALDYTDIPN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 243 KGVRKFTAAAMVQSAFTAPHVteFLTVD--VTATMELLARLKGNRTFEGFK---LTPLTIaaKAVLVALRNNPSLNSRWd 317
Cdd:PLN02744 315 TQIRKVTASRLLQSKQTIPHY--YLTVDtrVDKLMALRSQLNSLQEASGGKkisVNDLVI--KAAALALRKVPQCNSSW- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 318 eANQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNI-GVFGIDAG 396
Cdd:PLN02744 390 -TDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQF 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2187903916 397 TPILNPGEAAIVALGAVRK--APWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPamvMTMI 467
Cdd:PLN02744 469 CAIINPPQSAILAVGSAEKrvIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP---ESML 538
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
182-463 |
2.37e-51 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 176.14 E-value: 2.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 182 STPPVRKLARDLGIDLELVPGTGPGGLITREDVQNF-----------------SGTADELAVAPVAAGQGERETRTPIKG 244
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFikslksaptpaeaasvsSAQQAAKTAAPAAAPPKLEGKREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 245 VRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKGN-RTFEGFKLTPLTIAAKAVLVALRNNPSLNSRWDEANQEI 323
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 324 VQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTPILNPG 403
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 404 EAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPAMV 463
Cdd:PRK11857 244 ELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
181-460 |
5.31e-51 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 176.25 E-value: 5.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 181 RSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQNFSGTAdELAVAPVA--------------AGQGER---------- 236
Cdd:PRK14843 7 RATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTN-VVRISPLAkrialehniawqeiQGTGHRgkimkkdvla 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 237 ------ET--------------------------RTPIKGVRKFTAAAMVQSAFTAPHVTEFLTVDVTATMELLAR-LKG 283
Cdd:PRK14843 86 llpeniENdsikspaqiekveevpdnvtpygeieRIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 284 NRTFEGFKLTPLTIAAKAVLVALRNNPSLNSRWDEANQEIVQFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQ 363
Cdd:PRK14843 166 IMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 364 LTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTPILNPGEAAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDG 443
Cdd:PRK14843 246 VIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDG 325
|
330
....*....|....*..
gi 2187903916 444 EQGSRFLADLGAILSDP 460
Cdd:PRK14843 326 MAGAKFMKDLKELIETP 342
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-464 |
5.34e-37 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 141.43 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 8 EFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEvgkpivsfevddags 87
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVE--------------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 88 sngagsptagAGSAVGASAHGAPAASGVeavgTPAKREPNlvgygavvEHSGRPTRRAR-VQAPAAEQATVqAEVPAIPE 166
Cdd:PLN02226 158 ----------PGTKVAIISKSEDAASQV----TPSQKIPE--------TTDPKPSPPAEdKQKPKVESAPV-AEKPKAPS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 167 PVAEPQAevSGERPRSTPPvrklardlgidlelvpgtgpgglitredvqnfsgtadelavapvaagqgERETRTPIKGVR 246
Cdd:PLN02226 215 SPPPPKQ--SAKEPQLPPK-------------------------------------------------ERERRVPMTRLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 247 KFTAAAMVQSAFTAPHVTEFLTVDVTATMELLARLKgNRTFE--GFKLTPLTIAAKAVLVALRNNPSLNSRWDeaNQEIV 324
Cdd:PLN02226 244 KRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYK-DAFYEkhGVKLGLMSGFIKAAVSALQHQPVVNAVID--GDDII 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 325 QFNYVNLGIAAATPRGLTVPNIKDADQLSLRELSTALTQLTDTARAGKTSPSDLSGGTISITNIGVFGIDAGTPILNPGE 404
Cdd:PLN02226 321 YRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQ 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 405 AAIVALGAVRKAPWVVNDELAVRQVMSLSLSFDHRLVDGEQGSRFLADLGAILSDPAMVM 464
Cdd:PLN02226 401 SAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
5-80 |
1.72e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 104.76 E-value: 1.72e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2187903916 5 MIKEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSF 80
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
145-457 |
1.11e-25 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 110.75 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 145 ARVQAPAAEQATVQAEVPAIPEPVAEPQAEVSGERPRSTPPVRKLArdlgidlelvPGTGPGGLITRedvqnfSGTADEL 224
Cdd:PRK12270 40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPK----------PAAAAAAAAAP------AAPPAAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 225 AVAPVAAGQGERETrTPIKGVRKFTAAAMVQSaFTAPHVTEFLTVDVTATME-------LLARLKGNrtfegfKLTPLTI 297
Cdd:PRK12270 104 AAAAPAAAAVEDEV-TPLRGAAAAVAKNMDAS-LEVPTATSVRAVPAKLLIDnrivinnHLKRTRGG------KVSFTHL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 298 AAKAVLVALRNNPSLNSRWDEAN--QEIVQFNYVNLGIAAATP-----RGLTVPNIKDADQLSLRELSTALTQLTDTARA 370
Cdd:PRK12270 176 IGYALVQALKAFPNMNRHYAEVDgkPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 371 GKTSPSDLSGGTISITNIGVFGIDAGTPILNPGEAAIVALGAV------RKAPWVVNDELAVRQVMSLSLSFDHRLVDGE 444
Cdd:PRK12270 256 GKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMeypaefQGASEERLAELGISKVMTLTSTYDHRIIQGA 335
|
330
....*....|...
gi 2187903916 445 QGSRFLADLGAIL 457
Cdd:PRK12270 336 ESGEFLRTIHQLL 348
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
7-77 |
2.13e-25 |
|
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: 98.63 E-value: 2.13e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2187903916 7 KEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPI 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
7-78 |
6.55e-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: 78.02 E-value: 6.55e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2187903916 7 KEFRLPDLGEGLTESeILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIV 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 ... |
180-215 |
5.81e-13 |
|
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: 62.70 E-value: 5.81e-13
10 20 30
....*....|....*....|....*....|....*.
gi 2187903916 180 PRSTPPVRKLARDLGIDLELVPGTGPGGLITREDVQ 215
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
5-77 |
3.43e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 64.58 E-value: 3.43e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2187903916 5 MIKEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPI 77
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
23-80 |
5.80e-10 |
|
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: 55.11 E-value: 5.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2187903916 23 ILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSF 80
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
10-80 |
3.32e-08 |
|
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: 50.52 E-value: 3.32e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2187903916 10 RLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSF 80
Cdd:cd06663 3 LIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
5-126 |
6.79e-07 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 51.46 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 5 MIKEFRLPDLGEGLTESEILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTV-VEVGKPIVSFEVD 83
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLLEE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2187903916 84 DAGSSNGAGSPTAGAGSAVGASAHGAPAASGVEAVGTPAKREP 126
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAP 123
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
29-72 |
8.42e-07 |
|
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: 47.81 E-value: 8.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2187903916 29 AVGDTVTLNQVIAEVETAKAVVELPSPFAGTV----AALHEQPGTVVE 72
Cdd:COG0509 46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVvevnEALEDDPELVNE 93
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
28-81 |
5.79e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 45.66 E-value: 5.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2187903916 28 VAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFE 81
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
30-65 |
5.82e-06 |
|
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: 44.83 E-value: 5.82e-06
10 20 30
....*....|....*....|....*....|....*.
gi 2187903916 30 VGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHE 65
Cdd:cd06848 39 VGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVNE 74
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
23-81 |
9.04e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 44.83 E-value: 9.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2187903916 23 ILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFE 81
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK01202 |
PRK01202 |
glycine cleavage system protein GcvH; |
30-70 |
6.55e-04 |
|
glycine cleavage system protein GcvH;
Pssm-ID: 234918 Cd Length: 127 Bit Score: 39.76 E-value: 6.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2187903916 30 VGDTVTLNQVIAEVETAKAVVELPSPFAGTV----AALHEQPGTV 70
Cdd:PRK01202 47 VGDEVKAGETFGVVESVKAASDIYAPVSGEVvevnEALEDSPELV 91
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
28-81 |
9.83e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.07 E-value: 9.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2187903916 28 VAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVSFE 81
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
23-79 |
1.19e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 39.02 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2187903916 23 ILSWKVAVGDTVTLNQVIAEVETAKAVVELPSPFAGTVAALHEQPGTVVEVGKPIVS 79
Cdd:PRK06549 72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLIT 128
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
91-231 |
3.91e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.86 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187903916 91 AGSPTAGAGSAVGASAHGAPAASGVEAVGtPAKREPNLVGYGAVVEHSGRPTRRARVQAPAAEQATVQAEVPAIPEPVAE 170
Cdd:PRK12323 394 AAAPAPAAPPAAPAAAPAAAAAARAVAAA-PARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPV 472
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2187903916 171 PQAEVSGERPRSTPPVRKLARDLGIDLELVPGTGP---------------GGLITREDVQNFSGTADELAVAPVAA 231
Cdd:PRK12323 473 AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFAspapaqpdaapagwvAESIPDPATADPDDAFETLAPAPAAA 548
|
|
| |
