|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
1-366 |
2.28e-153 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 435.49 E-value: 2.28e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 1 MERDKVRATPAARALARRLGVDIYNVTGTGYKGRIHRDDIAGYNYEDKIHISPLARRIADAHNIDLKGLQGTGHRNKIMK 80
Cdd:PRK14843 1 MADDKLRATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 81 DDVLKLIEDPElramlDRDYFAeaitltkamPSAEKQAAQKIEKKLSVSrpevaGDTETVPMTQMRKIIARRMSESFFGI 160
Cdd:PRK14843 81 KDVLALLPENI-----ENDSIK---------SPAQIEKVEEVPDNVTPY-----GEIERIPMTPMRKVIAQRMVESYLTA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 161 PTFIQTWEVDMSEMLMLRNRLMGPIKDKTGRKLTVTDLISMSVVKTLMNHKYINASINAEGTELTFHNYVNLGVAVGMDE 240
Cdd:PRK14843 142 PTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 241 GLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVSSTKDRIVP 320
Cdd:PRK14843 222 GLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVV 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2196777743 321 VNGEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTLLI 366
Cdd:PRK14843 302 VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
50-366 |
5.69e-106 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 317.12 E-value: 5.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 50 HISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLIedpelramldrdyfaeaitltkampSAEKQAAQKIEKKLSVS 129
Cdd:PRK11856 126 KASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA-------------------------AAAAPAAAAAAAAAAAP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 130 RPEVAGDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRLmgpikDKTGRKLTVTDLISMSVVKTLMN 209
Cdd:PRK11856 181 PAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----KAIGVKLTVTDFLIKAVALALKK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 210 HKYINASINAEGteLTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNL 289
Cdd:PRK11856 256 FPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNL 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2196777743 290 GMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTLLI 366
Cdd:PRK11856 334 GMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
153-365 |
5.40e-88 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 264.02 E-value: 5.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 153 MSESFFGIPTFIQTWEVDMSEMLMLRNRLmGPIKDKTGRKLTVTDLISMSVVKTLMNHKYINASINAEGTELTFHNYVNL 232
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREEL-KEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 233 GVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVS 312
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2196777743 313 STKDRIVPVNGEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTLL 365
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
47-365 |
1.39e-81 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 258.60 E-value: 1.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 47 DKIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKliedpelramldrdyFAEAITLTKAMPSAEKQAAQKIEKKL 126
Cdd:PRK11855 241 KAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQA---------------FVKGAMSAAAAAAAAAAAAGGGGLGL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 127 SVSrPEVA----GDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRlMGPIKDKTGRKLTVTDLISMS 202
Cdd:PRK11855 306 LPW-PKVDfskfGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQ-LKKEAEKAGVKLTMLPFFIKA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 203 VVKTLMNHKYINASINAEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGS 282
Cdd:PRK11855 384 VVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGG 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 283 TFSISNLGMYGVDEFTAIINQPNAAILSVSstKDRIVPVN--GEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLED 360
Cdd:PRK11855 464 CFTISSLGGIGGTAFTPIINAPEVAILGVG--KSQMKPVWdgKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLAD 541
|
....*
gi 2196777743 361 PVTLL 365
Cdd:PRK11855 542 PRRML 546
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
46-366 |
7.38e-78 |
|
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: 245.86 E-value: 7.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 46 EDKIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLIEdpelramldrdyfaeaitltKAMPSAEKQAAQKIEKK 125
Cdd:TIGR01349 137 GDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVP--------------------QSPASANQQAAATTPAT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 126 LSVSRPEVAGDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRLMGPIKDKTgrKLTVTDLISMSVVK 205
Cdd:TIGR01349 197 YPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEVY--KLSVNDFIIKASAL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 206 TLMNHKYINASINaeGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFS 285
Cdd:TIGR01349 275 ALREVPEANSSWT--DNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 286 ISNLGMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGEA---VIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPV 362
Cdd:TIGR01349 353 ISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEkgfAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPI 432
|
....
gi 2196777743 363 TLLI 366
Cdd:TIGR01349 433 EMLL 436
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
46-365 |
1.04e-67 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 224.50 E-value: 1.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 46 EDKIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLIEDpelramldrdyfaeaiTLTKAMPSAEKQAAQKIEKK 125
Cdd:PRK11854 325 DAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKD----------------AVKRAEAAPAAAAAGGGGPG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 126 L---SVSRPEVAGDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRLMGP-IKDKTGRKLTVTDLISM 201
Cdd:PRK11854 389 LlpwPKVDFSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEaEKRKLGVKITPLVFIMK 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 202 SVVKTLMNHKYINASINAEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTG 281
Cdd:PRK11854 469 AVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQG 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 282 STFSISNLGMYGVDEFTAIINQPNAAILSVSstKDRIVPV-NGEA-VIRPIMKISLTCDHRIIDGLTAAKFMADLKALLE 359
Cdd:PRK11854 549 GCFTISSIGGLGTTHFTPIVNAPEVAILGVS--KSAMEPVwNGKEfAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
....*.
gi 2196777743 360 DPVTLL 365
Cdd:PRK11854 627 DIRRLV 632
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
46-366 |
3.14e-67 |
|
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: 217.29 E-value: 3.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 46 EDKIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLiedpelramldrdyfaeaitlTKAMPSAEKQAAQKIEKK 125
Cdd:TIGR01347 108 ANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK---------------------TEAPASAQPPAAAAAAAA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 126 -LSVSRPEvagdtETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRLMGPIKDKTGRKLTVTDLISMSVV 204
Cdd:TIGR01347 167 pAAATRPE-----ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 205 KTLMNHKYINASInaEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTF 284
Cdd:TIGR01347 242 AALKRFPEVNAEI--DGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 285 SISNLGMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTL 364
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
..
gi 2196777743 365 LI 366
Cdd:TIGR01347 400 LL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
46-365 |
4.25e-65 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 212.00 E-value: 4.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 46 EDKIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLIEDPelramldrdyfaeaitltKAMPSAEKQAAQKIEKK 125
Cdd:PRK05704 110 QSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAA------------------AAAPAAPAAAAPAAAPA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 126 LSVSRPEvagdtETVPMTQMRKIIARRMSESFFG---IPTFIqtwEVDMSEMLMLRNRLmgpiKD----KTGRKLTVtdl 198
Cdd:PRK05704 172 PLGARPE-----ERVPMTRLRKTIAERLLEAQNTtamLTTFN---EVDMTPVMDLRKQY----KDafekKHGVKLGF--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 199 isMS-----VVKTLMNHKYINASInaEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKK 273
Cdd:PRK05704 237 --MSffvkaVVEALKRYPEVNASI--DGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGK 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 274 LLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGEAVIRPIMKISLTCDHRIIDGLTAAKFMAD 353
Cdd:PRK05704 313 LSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVT 392
|
330
....*....|..
gi 2196777743 354 LKALLEDPVTLL 365
Cdd:PRK05704 393 IKELLEDPERLL 404
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
50-366 |
1.91e-60 |
|
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: 203.57 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 50 HISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLIEDPELRAMldrdyfAEAITLTKAMPSAEKQAAQKIEKklsvs 129
Cdd:TIGR01348 246 HAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQ------AAAASAAGGAPGALPWPNVDFSK----- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 130 rpevAGDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRlMGPIKDKTGRKLTVTDLISMSVVKTLMN 209
Cdd:TIGR01348 315 ----FGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQ-QNAAVEKEGVKLTVLHILMKAVAAALKK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 210 HKYINASINAEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNL 289
Cdd:TIGR01348 390 FPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSL 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2196777743 290 GMYGVDEFTAIINQPNAAILSVSstKDRIVPV-NGEA-VIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTLLI 366
Cdd:TIGR01348 470 GGIGGTAFTPIVNAPEVAILGVS--KSGMEPVwNGKEfEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
9-360 |
1.80e-56 |
|
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: 193.69 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 9 TPAARALARRLGVDIYNVTGTGYKGRIHrddiagynyedkihisplarriadahnidlkglqgtghrnkimKDDVLKLIE 88
Cdd:TIGR02927 269 TPLVRKLAKDKGVDLSTVKGTGVGGRIR-------------------------------------------KQDVLAAAK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 89 DPElramldrdyfAEAITLTKAMPSAEKQAAQKIEKKLSVSRPEVAGDTETvpMTQMRKIIARRMSESFFGIPTFIQTWE 168
Cdd:TIGR02927 306 AAE----------EARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQK--MNRIRQITADKTIESLQTSAQLTQVHE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 169 VDMSEMLMLRNRLMGPIKDKTGRKLTVTDLISMSVVKTLMNHKYINASINAEGTELTFHNYVNLGVAVGMDEGLLVPVVK 248
Cdd:TIGR02927 374 VDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIH 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 249 NADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVSSTKDR---IVPVNGEA 325
Cdd:TIGR02927 454 NAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRprvIKDEDGGE 533
|
330 340 350
....*....|....*....|....*....|....*..
gi 2196777743 326 VI--RPIMKISLTCDHRIIDGLTAAKFMADLKALLED 360
Cdd:TIGR02927 534 SIaiRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
46-366 |
2.32e-56 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 192.38 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 46 EDKIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLkliedpelramldrDYFAEAITLTKAMPSAEKQAAqkiekk 125
Cdd:PLN02744 246 GDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIE--------------DYLASGGKGATAPPSTDSKAP------ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 126 lsvsrpevAGDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRLmGPIKDKTGRK-LTVTDLISMSVV 204
Cdd:PLN02744 306 --------ALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQL-NSLQEASGGKkISVNDLVIKAAA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 205 KTLMNHKYINASINAEGTElTFHNyVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTF 284
Cdd:PLN02744 377 LALRKVPQCNSSWTDDYIR-QYHN-VNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTF 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 285 SISNL-GMYGVDEFTAIINQPNAAILSVSSTKDRIVP--VNGEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDP 361
Cdd:PLN02744 455 TVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPgsGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
|
....*
gi 2196777743 362 VTLLI 366
Cdd:PLN02744 535 ESMLL 539
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
109-366 |
9.28e-55 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 185.27 E-value: 9.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 109 KAMPSAEKQAAQKIEKKLSVSRPEVA-------------GDTET-VPMTQMRKIIARRMSES---FFGIPTFIqtwEVDM 171
Cdd:PTZ00144 147 AAAPTPEPPAASKPTPPAAAKPPEPApaakppptpvaraDPRETrVPMSRMRQRIAERLKASqntCAMLTTFN---ECDM 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 172 SEMLMLRNRLMGPIKDKTGRKLTVTDLISMSVVKTLMNHKYINASInaEGTELTFHNYVNLGVAVGMDEGLLVPVVKNAD 251
Cdd:PTZ00144 224 SALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYI--DGDEIVYRNYVDISVAVATPTGLVVPVIRNCE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 252 KMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGEAVIRPIM 331
Cdd:PTZ00144 302 NKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIM 381
|
250 260 270
....*....|....*....|....*....|....*
gi 2196777743 332 KISLTCDHRIIDGLTAAKFMADLKALLEDPVTLLI 366
Cdd:PTZ00144 382 YLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
48-364 |
2.10e-53 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 178.45 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 48 KIHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKLIEDPElramldrdyfaeaiTLTKAMPSAEKQAAQKIEKKLS 127
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLK--------------SAPTPAEAASVSSAQQAAKTAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 128 VSRPEVAGDTETVPMTQMRKIIARRMSESFFGIPTFIQTWEVDMSEMLMLRNRLMGPIKDKTGRKLTVTDLISMSVVKTL 207
Cdd:PRK11857 67 PAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 208 MNHKYINASINAEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSIS 287
Cdd:PRK11857 147 KEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTIT 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2196777743 288 NLGMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGEAVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTL 364
Cdd:PRK11857 227 NYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
106-366 |
1.03e-43 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 157.22 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 106 TLTKAMPSAEKQAAQKIEK----------------KLSVSRPEVA-GDTET-VPMTQMRKIIARRMSES---FFGIPTFI 164
Cdd:PLN02226 185 TDPKPSPPAEDKQKPKVESapvaekpkapssppppKQSAKEPQLPpKERERrVPMTRLRKRVATRLKDSqntFALLTTFN 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 165 qtwEVDMSEMLMLRNRLMGPIKDKTGRKLTVTDLISMSVVKTLMNHKYINASInaEGTELTFHNYVNLGVAVGMDEGLLV 244
Cdd:PLN02226 265 ---EVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVI--DGDDIIYRDYVDISIAVGTSKGLVV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 245 PVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVSSTKDRIVPVNGE 324
Cdd:PLN02226 340 PVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGS 419
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2196777743 325 AVIRPIMKISLTCDHRIIDGLTAAKFMADLKALLEDPVTLLI 366
Cdd:PLN02226 420 VVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
52-366 |
3.12e-37 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 138.70 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 52 SPLARRIADAHNIDLKGLQGTGHRNKIMKDDVLKliedpelramldrdyFAEAITLTKAMPSAE--KQAAQKIEKKLSVS 129
Cdd:PLN02528 113 TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLK---------------YAAQKGVVKDSSSAEeaTIAEQEEFSTSVST 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 130 RPEVAGDTETVPMTQMRKIIARRMSESFfGIPTFIQTWEVDMSEMLMLRnRLMGPIKDKTGRKLTVTDLISMSVVKTLMN 209
Cdd:PLN02528 178 PTEQSYEDKTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVELK-ASFQENNTDPTVKHTFLPFLIKSLSMALSK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 210 HKYINASINAEGTELTFHNYVNLGVAVGMDEGLLVPVVKNADKMSLSELVVSMKDLAERTFSKKLLPDEQTGSTFSISNL 289
Cdd:PLN02528 256 YPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 290 GMYGVDEFTAIINQPNAAILSVS--------STKDRIVPVNgeavirpIMKISLTCDHRIIDGLTAAKFMADLKALLEDP 361
Cdd:PLN02528 336 GAIGGKFGSPVLNLPEVAIIALGriqkvprfVDDGNVYPAS-------IMTVTIGADHRVLDGATVARFCNEWKSYVEKP 408
|
....*
gi 2196777743 362 VTLLI 366
Cdd:PLN02528 409 ELLML 413
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
112-358 |
1.10e-16 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 81.86 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 112 PSAEKQAAQKIEKKLSVSRPEVAGDTETVPMTQMRKIIARRMSESFfGIPTfiQTWEVDMSEMLMLRNRLMgpIKD--KT 189
Cdd:PRK12270 90 AAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASL-EVPT--ATSVRAVPAKLLIDNRIV--INNhlKR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 190 GR--KLTVTDLISMSVVKTL-----MNHKYinASINAEGTELTFHnYVNLGVAVGM--DEG---LLVPVVKNADKMSLSE 257
Cdd:PRK12270 165 TRggKVSFTHLIGYALVQALkafpnMNRHY--AEVDGKPTLVTPA-HVNLGLAIDLpkKDGsrqLVVPAIKGAETMDFAQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196777743 258 LVVSMKDLAERTFSKKLLPDEQTGSTFSISNLGMYGVDEFTAIINQPNAAILSVSS----------TKDRIvpvnGEAVI 327
Cdd:PRK12270 242 FWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefqgaSEERL----AELGI 317
|
250 260 270
....*....|....*....|....*....|.
gi 2196777743 328 RPIMKISLTCDHRIIDGLTAAKFMADLKALL 358
Cdd:PRK12270 318 SKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
6-40 |
1.05e-11 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 58.85 E-value: 1.05e-11
10 20 30
....*....|....*....|....*....|....*
gi 2196777743 6 VRATPAARALARRLGVDIYNVTGTGYKGRIHRDDI 40
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
49-84 |
1.58e-10 |
|
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: 55.39 E-value: 1.58e-10
10 20 30
....*....|....*....|....*....|....*.
gi 2196777743 49 IHISPLARRIADAHNIDLKGLQGTGHRNKIMKDDVL 84
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| |
