|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
214-637 |
2.10e-144 |
|
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: 426.52 E-value: 2.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 214 VLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAES 293
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 294 IEAIKS----------------------SSAGSSEVDTVKEVPDSVVDKPTERKAGFTKI--SPAAKLLILEHGLEASSI 349
Cdd:TIGR01349 81 VADAFKnyklessaspapkpseiaptapPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIfaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 350 EASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSSTSKPSVTQSDN-NYEDFPNSQIRKIIAKRLLESKQ 428
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSP-----------ASANQQAAATTPATYPAAAPVSTgSYEDVPLSNIRKIIAKRLLESKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 429 KIPHLYLQSDVVLDPLLAFRKELQE--NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEK 506
Cdd:TIGR01349 230 TIPHYYVSIECNVDKLLALRKELNAmaSEVYKLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 507 GLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVvep 586
Cdd:TIGR01349 308 GLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV--- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15231159 587 VIGLDGIEKP-SVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:TIGR01349 385 AVVDNDEEKGfAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
217-637 |
1.84e-132 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 394.93 E-value: 1.84e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 217 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIVEDAESIEA 296
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEAEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 297 IKSSSAGSSEVDTVKEVPDSVVDKPTER-------KAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIas 369
Cdd:PRK11856 86 AAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 370 gkaskssastkkkQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK 449
Cdd:PRK11856 164 -------------AAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 450 ELQENhGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVK 529
Cdd:PRK11856 231 QLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 530 ELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGnkVVEPVIGLDGIEkpsVVTKMNVTLSAD 609
Cdd:PRK11856 308 DLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI--VERPVVVDGEIV---VRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 15231159 610 HRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
423-636 |
9.79e-82 |
|
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: 256.70 E-value: 9.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 423 LLESKQKIPHLYLQSDVVLDPLLAFRKELQENH---GVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDIS 499
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 500 IAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGR 579
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231159 580 GNKVvePVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLL 636
Cdd:pfam00198 161 IRKR--PVVVDGEIV---VRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
90-173 |
1.37e-31 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 128.11 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKN 169
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
....
gi 15231159 170 VPAT 173
Cdd:PRK11892 87 AGAA 90
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
90-160 |
2.03e-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: 105.18 E-value: 2.03e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 160
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
213-287 |
2.64e-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: 99.40 E-value: 2.64e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231159 213 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 287
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
90-161 |
1.34e-24 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 97.44 E-value: 1.34e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIMV 161
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
213-288 |
1.28e-22 |
|
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: 91.67 E-value: 1.28e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231159 213 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIV 288
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
86-160 |
4.84e-15 |
|
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: 70.32 E-value: 4.84e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231159 86 TVLAMPALSPTMsHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 160
Cdd:pfam00364 1 TEIKSPMIGESV-REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
214-637 |
2.10e-144 |
|
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: 426.52 E-value: 2.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 214 VLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAES 293
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 294 IEAIKS----------------------SSAGSSEVDTVKEVPDSVVDKPTERKAGFTKI--SPAAKLLILEHGLEASSI 349
Cdd:TIGR01349 81 VADAFKnyklessaspapkpseiaptapPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIfaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 350 EASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSSTSKPSVTQSDN-NYEDFPNSQIRKIIAKRLLESKQ 428
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSP-----------ASANQQAAATTPATYPAAAPVSTgSYEDVPLSNIRKIIAKRLLESKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 429 KIPHLYLQSDVVLDPLLAFRKELQE--NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEK 506
Cdd:TIGR01349 230 TIPHYYVSIECNVDKLLALRKELNAmaSEVYKLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 507 GLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVvep 586
Cdd:TIGR01349 308 GLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV--- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15231159 587 VIGLDGIEKP-SVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:TIGR01349 385 AVVDNDEEKGfAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
217-637 |
1.84e-132 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 394.93 E-value: 1.84e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 217 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIVEDAESIEA 296
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEAEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 297 IKSSSAGSSEVDTVKEVPDSVVDKPTER-------KAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIas 369
Cdd:PRK11856 86 AAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 370 gkaskssastkkkQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK 449
Cdd:PRK11856 164 -------------AAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 450 ELQENhGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVK 529
Cdd:PRK11856 231 QLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 530 ELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGnkVVEPVIGLDGIEkpsVVTKMNVTLSAD 609
Cdd:PRK11856 308 DLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI--VERPVVVDGEIV---VRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 15231159 610 HRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
207-637 |
1.27e-127 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 386.90 E-value: 1.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 207 SDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIAL 286
Cdd:PLN02744 107 SDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 287 IVEDAESIEAIK----SSSAGSS--------------EVDTVKEVPDSVVDKPTERKAGFTKI--SPAAKLLILEHGLEA 346
Cdd:PLN02744 187 TVEEEEDIGKFKdykpSSSAAPAapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIfaSPLARKLAEDNNVPL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 347 SSIEASGPYGTLLKSDVVAAIasgkaskssastkkKQPSKETPSKSSSTSKPsvtqSDNNYEDFPNSQIRKIIAKRLLES 426
Cdd:PLN02744 267 SSIKGTGPDGRIVKADIEDYL--------------ASGGKGATAPPSTDSKA----PALDYTDIPNTQIRKVTASRLLQS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 427 KQKIPHLYLQSDVVLDPLLAFRKEL---QENHGVK-VSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAV 502
Cdd:PLN02744 329 KQTIPHYYLTVDTRVDKLMALRSQLnslQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTDDY--IRQYHNVNINVAV 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 503 ATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNL-GMYPVDNFCAIINPPQAGILAVGRGN 581
Cdd:PLN02744 407 QTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAE 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231159 582 KVVEPVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:PLN02744 487 KRVIPGSGPDQYN---FASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
100-637 |
2.46e-86 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 279.79 E-value: 2.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 100 GNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM-VEEEDDIKNVPATIEggr 178
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGLLAVIeAAGAAAAAAAPAAAA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 179 dgKEETSAHQVMKPDESTQQKSSIQPDASDLPphvvLEMPALSpTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEF 258
Cdd:PRK11855 92 --APAAAAAAAPAPAAAAPAAAAAAAGGGVVE----VKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 259 ESLEEGYLAKILIPEGSKdVAVGKPIALIvEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKI------- 331
Cdd:PRK11855 165 PSPVAGVVKEIKVKVGDK-VSVGSLLVVI-EVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAaaapgka 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 332 ---SPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSSTSKPSVTQSDNNYE 408
Cdd:PRK11855 243 phaSPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAM-----------SAAAAAAAAAAAAGGGGLGLLPWPKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 409 DF---------PNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQ---ENHGVKVSVNDIVIKAVAVALRNV 476
Cdd:PRK11855 312 DFskfgeietkPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKkeaEKAGVKLTMLPFFIKAVVAALKEF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 477 RQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLG 556
Cdd:PRK11855 392 PVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 557 MYPVDNFCAIINPPQAGILAVGRGnkVVEPVigldgIEKPSVVTK--MNVTLSADHRIFDGQVGASFMSELRSNFEDVRR 634
Cdd:PRK11855 472 GIGGTAFTPIINAPEVAILGVGKS--QMKPV-----WDGKEFVPRlmLPLSLSYDHRVIDGATAARFTNYLKQLLADPRR 544
|
...
gi 15231159 635 LLL 637
Cdd:PRK11855 545 MLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
423-636 |
9.79e-82 |
|
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: 256.70 E-value: 9.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 423 LLESKQKIPHLYLQSDVVLDPLLAFRKELQENH---GVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDIS 499
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 500 IAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGR 579
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231159 580 GNKVvePVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLL 636
Cdd:pfam00198 161 IRKR--PVVVDGEIV---VRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
218-637 |
1.20e-72 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 239.74 E-value: 1.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 218 PALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSkDVAVGKPIALIVEDAESieAI 297
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAAA--GA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 298 KSSSAGSSEVDTVKEVPDSVVDKPTERKAGftkISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGkaskssa 377
Cdd:PRK05704 85 AAAAAAAAAAAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAA------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 378 stkkkqPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQE---- 453
Cdd:PRK05704 155 ------AAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDafek 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 454 NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEkgDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQ 533
Cdd:PRK05704 229 KHGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 534 KARSGKLAPHEFQGGTFSISNLGMY------PvdnfcaIINPPQAGILAVgrgNKVVEPVIGLDGiekpSVVTK--MNVT 605
Cdd:PRK05704 307 KARDGKLSIEELTGGTFTITNGGVFgslmstP------IINPPQSAILGM---HKIKERPVAVNG----QIVIRpmMYLA 373
|
410 420 430
....*....|....*....|....*....|..
gi 15231159 606 LSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:PRK05704 374 LSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
215-637 |
1.74e-68 |
|
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: 228.46 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 215 LEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIVEDAESI 294
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 295 EAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAgftkiSPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAiasgkask 374
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAASAAAAPTAAANRPSL-----SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 375 sSASTKKKQPSKETPSKSSSTskpsvtQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQE- 453
Cdd:TIGR01347 149 -TEAPASAQPPAAAAAAAAPA------AATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEe 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 454 ---NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEkgDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKE 530
Cdd:TIGR01347 222 fekKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIAD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 531 LAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILavgrgnkvvepviGLDGI-EKPSVVTK-------M 602
Cdd:TIGR01347 300 LGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAIL-------------GMHGIkERPVAVNGqieirpmM 366
|
410 420 430
....*....|....*....|....*....|....*
gi 15231159 603 NVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:TIGR01347 367 YLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
100-637 |
1.51e-67 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 232.20 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 100 GNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdipVNEPIAIMVEEeddiknvpatieggrD 179
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK---VSTGSLIMVFE---------------V 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 180 GKEETSAHQVMKPDESTQQKSSIQPDASDLpphvvlEMPALSPTmnQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFE 259
Cdd:PRK11854 180 AGEAPAAAPAAAEAAAPAAAPAAAAGVKDV------NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 260 SLEEGYLAKILIPEGSKdVAVGKPIAlIVEDAESIEAIKSSSAGSSE---VDTVKEVPDSVVDKPTERKAGFTK------ 330
Cdd:PRK11854 252 APFAGTVKEIKVNVGDK-VKTGSLIM-RFEVEGAAPAAAPAKQEAAApapAAAKAEAPAAAPAAKAEGKSEFAEndayvh 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 331 ISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKaskssastkkkqPSKETPSKSSSTSKPSVTQSDNNYEDF 410
Cdd:PRK11854 330 ATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAV------------KRAEAAPAAAAAGGGGPGLLPWPKVDF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 411 ---------PNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKE-----LQENHGVKVSVNDIVIKAVAVALRNV 476
Cdd:PRK11854 398 skfgeieevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQqnaeaEKRKLGVKITPLVFIMKAVAAALEQM 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 477 RQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLG 556
Cdd:PRK11854 478 PRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIG 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 557 MYPVDNFCAIINPPQAGILAVGRgnKVVEPVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLL 636
Cdd:PRK11854 558 GLGTTHFTPIVNAPEVAILGVSK--SAMEPVWNGKEFA---PRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLV 632
|
.
gi 15231159 637 L 637
Cdd:PRK11854 633 L 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
90-631 |
9.16e-66 |
|
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: 226.05 E-value: 9.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEgSKDIPVNEPIAIMVEE-EDDIK 168
Cdd:TIGR02927 7 MPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPgEAGSE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 169 NVPATIEGGRDGKEETSAHQVmKPDESTQQKSSIQPDASDLPPHVvlEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGE 248
Cdd:TIGR02927 86 PAPAAPEPEAAPEPEAPAPAP-TPAAEAPAPAAPQAGGSGEATEV--KMPELGESVTEGTVTSWLKAVGDTVEVDEPLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 249 IETDKATLEFESLEEGYLAKILIPEgSKDVAVGKPIALI------VEDAESIEAIKSSSAGSSEV-----DTVKEVPDSV 317
Cdd:TIGR02927 163 VSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIgdanaaPAEPAEEEAPAPSEAGSEPApdpaaRAPHAAPDPP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 318 VDKPTERK-------------AGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAiaSGKASKSSASTKKKQP 384
Cdd:TIGR02927 242 APAPAPAKtaapaaaapvssgDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAA--AKAAEEARAAAAAPAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 385 SKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK----ELQENHGVKVS 460
Cdd:TIGR02927 320 AAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRAraknDFLEKNGVNLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 461 VNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKL 540
Cdd:TIGR02927 400 FLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 541 APHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVVEPVIGLDGIEKPSVVTKMNVTLSADHRIFDGQVGAS 620
Cdd:TIGR02927 480 KPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGR 559
|
570
....*....|.
gi 15231159 621 FMSELRSNFED 631
Cdd:TIGR02927 560 FLTTIKKRLEE 570
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
98-637 |
5.71e-58 |
|
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: 204.34 E-value: 5.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 98 SHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIMVEEEDDIKNVPATIEGG 177
Cdd:TIGR01348 12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDT-LPVGGVIATLEVGAGAQAQAEAKKEAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 178 ---RDGKEETSAHQVMKPDEStqQKSSIQ----PDASDLPPHVVLEMPAlsptmnqgniakwwkKEGDKIEVGDVIGEIE 250
Cdd:TIGR01348 91 papTAGAPAPAAQAQAAPAAG--QSSGVQevtvPDIGDIEKVTVIEVLV---------------KVGDTVSADQSLITLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 251 TDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIaLIVEDAESIEAI-----KSSSAGSSEVDTVKEVP----------D 315
Cdd:TIGR01348 154 SDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLI-LTLSVAGSTPATapapaSAQPAAQSPAATQPEPAaapaaakaqaP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 316 SVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSST 395
Cdd:TIGR01348 232 APQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPS-----------VRAQAAAASAAGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 396 SKPSVTQSDNNYEDF------PNSQIRKIIAKRLLESKQKIPHL--YLQSDVVldPLLAFRKELQ---ENHGVKVSVNDI 464
Cdd:TIGR01348 301 APGALPWPNVDFSKFgeveevDMSRIRKISGANLTRNWTMIPHVthFDKADIT--EMEAFRKQQNaavEKEGVKLTVLHI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 465 VIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHE 544
Cdd:TIGR01348 379 LMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 545 FQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGnkVVEPVigLDGIE-KPSVVtkMNVTLSADHRIFDGQVGASFMS 623
Cdd:TIGR01348 459 MQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKS--GMEPV--WNGKEfEPRLM--LPLSLSYDHRVIDGADAARFTT 532
|
570
....*....|....
gi 15231159 624 ELRSNFEDVRRLLL 637
Cdd:TIGR01348 533 YICESLADIRRLLL 546
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
213-637 |
1.44e-55 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 194.52 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 213 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSkDVAVGKPIalivedae 292
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPL-------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 293 sieaiksssagsSEVDTVKEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASgpygtllksdvvaaiasgka 372
Cdd:PTZ00144 116 ------------SEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPP-------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 373 skssastkkKQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQ 452
Cdd:PTZ00144 164 ---------AAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 453 EN----HGVKVSVNDIVIKAVAVALRNVRQANAFWDaeKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEV 528
Cdd:PTZ00144 235 DDfqkkHGVKLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 529 KELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGIL--------AVGRGNKVV-EPVigldgiekpsvv 599
Cdd:PTZ00144 313 ADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhaikkrPVVVGNEIViRPI------------ 380
|
410 420 430
....*....|....*....|....*....|....*...
gi 15231159 600 tkMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:PTZ00144 381 --MYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
231-637 |
1.02e-47 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 172.98 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 231 KWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKP-IALIVEDA--ESIEAIKSSSAGSsev 307
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETlLKIMVEDSqhLRSDSLLLPTDSS--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 308 dtvkEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKE 387
Cdd:PLN02528 93 ----NIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSAEEATIAEQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 388 TPSKSSSTskpsvTQSDNNYED--FPNSQIRKIIAKRLLESKQkIPHLYLQSDVVLDPLLAFRKELQEN---HGVKVSVN 462
Cdd:PLN02528 169 EEFSTSVS-----TPTEQSYEDktIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQENntdPTVKHTFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 463 DIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAP 542
Cdd:PLN02528 243 PFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 543 HEFQGGTFSISNLG------MYPVdnfcaiINPPQAGILAVGRGNKVVEPVIglDGIEKPSVVtkMNVTLSADHRIFDGQ 616
Cdd:PLN02528 323 EDITGGTITLSNIGaiggkfGSPV------LNLPEVAIIALGRIQKVPRFVD--DGNVYPASI--MTVTIGADHRVLDGA 392
|
410 420
....*....|....*....|.
gi 15231159 617 VGASFMSELRSNFEDVRRLLL 637
Cdd:PLN02528 393 TVARFCNEWKSYVEKPELLML 413
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
330-637 |
1.51e-46 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 167.77 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 330 KISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIAsgkaskssastkkkqPSKETPSKSSSTSKPSVTQSDNN--- 406
Cdd:PRK14843 50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLP---------------ENIENDSIKSPAQIEKVEEVPDNvtp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 407 ---YEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKEL----QENHGVKVSVNDIVIKAVAVALRNVRQA 479
Cdd:PRK14843 115 ygeIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVlepiMEATGKKTTVTDLLSLAVVKTLMKHPYI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 480 NAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYP 559
Cdd:PRK14843 195 NASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 560 VDNFCAIINPPQAGILAVGrgnkvvepviglDGIEKPSVVTK-------MNVTLSADHRIFDGQVGASFMSELRSNFEDV 632
Cdd:PRK14843 275 VQSFGPIINQPNSAILGVS------------STIEKPVVVNGeivirpiMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
....*
gi 15231159 633 RRLLL 637
Cdd:PRK14843 343 ISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
194-637 |
3.38e-41 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 156.07 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 194 ESTQQKSSIQPDASDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPE 273
Cdd:PLN02226 73 VSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 274 GSKdvavgkpialiVEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPterkagftkispaakllilehgleassieaSG 353
Cdd:PLN02226 153 GDT-----------VEPGTKVAIISKSEDAASQVTPSQKIPETTDPKP------------------------------SP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 354 PYGTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSKssstskpsvtqSDNNYEDFPNSQIRKIIAKRLLESKQKIPHL 433
Cdd:PLN02226 192 PAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLP-----------PKERERRVPMTRLRKRVATRLKDSQNTFALL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 434 YLQSDVVLDPLLAFRKELQ----ENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEkgDIVMCDSVDISIAVATEKGLM 509
Cdd:PLN02226 261 TTFNEVDMTNLMKLRSQYKdafyEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 510 TPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILavGRGNKVVEP-VI 588
Cdd:PLN02226 339 VPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAIL--GMHSIVSRPmVV 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15231159 589 GLDGIEKPsvvtKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 637
Cdd:PLN02226 417 GGSVVPRP----MMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
217-336 |
1.11e-37 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 145.83 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 217 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAESIEA 296
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15231159 297 IKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKISPAAK 336
Cdd:PRK11892 87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAE 126
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
330-630 |
4.44e-34 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 131.84 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 330 KISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSKSSSTSKPSVTQSDNNyed 409
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 410 fPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK----ELQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDA 485
Cdd:PRK11857 80 -KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKsvkdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 486 EKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLG----MYPVd 561
Cdd:PRK11857 159 ATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGsvgsLYGV- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231159 562 nfcAIINPPQAGILAVGrgnKVVEPVIGLDGIEKPSVVtkMNVTLSADHRIFDGQVGASFMSELRSNFE 630
Cdd:PRK11857 238 ---PVINYPELAIAGVG---AIIDKAIVKNGQIVAGKV--MHLTVAADHRWIDGATIGRFASRVKELLE 298
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
90-173 |
1.37e-31 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 128.11 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKN 169
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
....
gi 15231159 170 VPAT 173
Cdd:PRK11892 87 AGAA 90
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
90-160 |
2.03e-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: 105.18 E-value: 2.03e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 160
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
213-287 |
2.64e-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: 99.40 E-value: 2.64e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231159 213 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 287
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
90-161 |
1.34e-24 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 97.44 E-value: 1.34e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231159 90 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIMV 161
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
213-288 |
1.28e-22 |
|
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: 91.67 E-value: 1.28e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231159 213 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIV 288
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
86-164 |
1.28e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.91 E-value: 1.28e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231159 86 TVLAMPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSkDIPVNEPIAIMVEEE 164
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
217-297 |
9.54e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 79.22 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 217 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSkDVAVGKPIALIVEDAESIEA 296
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEVSDAE 85
|
.
gi 15231159 297 I 297
Cdd:PRK14875 86 I 86
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
86-149 |
2.21e-15 |
|
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: 71.32 E-value: 2.21e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231159 86 TVLAmPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSK 149
Cdd:cd06663 1 TILI-PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
86-160 |
4.84e-15 |
|
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: 70.32 E-value: 4.84e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231159 86 TVLAMPALSPTMsHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 160
Cdd:pfam00364 1 TEIKSPMIGESV-REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
218-276 |
1.28e-13 |
|
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: 66.31 E-value: 1.28e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231159 218 PALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSK 276
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
213-287 |
5.99e-13 |
|
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: 64.16 E-value: 5.99e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231159 213 VVLEMPALSPTMNQGnIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 287
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
100-148 |
2.45e-07 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 48.18 E-value: 2.45e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15231159 100 GNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGS 148
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
451-615 |
4.76e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 53.36 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 451 LQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGD--IVMCDSVDISIAVATEK-----GLMTPIIKNADQKSISA 523
Cdd:PRK12270 162 LKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGKptLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 524 ISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVG--------RGNKvvEPVIGLDGIEK 595
Cdd:PRK12270 242 FWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGameypaefQGAS--EERLAELGISK 319
|
170 180
....*....|....*....|
gi 15231159 596 psVVTkmnVTLSADHRIFDG 615
Cdd:PRK12270 320 --VMT---LTSTYDHRIIQG 334
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
92-147 |
5.27e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 46.37 E-value: 5.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231159 92 ALSPTMShGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEG 147
Cdd:PRK09282 524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
330-363 |
5.32e-05 |
|
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: 40.36 E-value: 5.32e-05
10 20 30
....*....|....*....|....*....|....
gi 15231159 330 KISPAAKLLILEHGLEASSIEASGPYGTLLKSDV 363
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
212-287 |
5.76e-04 |
|
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: 38.55 E-value: 5.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231159 212 HVVLEMPalsptmnqGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 287
Cdd:cd06850 1 EVTAPMP--------GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
108-148 |
1.25e-03 |
|
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: 39.49 E-value: 1.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15231159 108 KEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGS 148
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ 124
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
78-157 |
6.04e-03 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 39.05 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 78 SSTGPISQTVLAMPALSPTMSHGNVVKWMK---------------KEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKI 142
Cdd:PLN02983 176 PASSPPPTPASPPPAKAPKSSHPPLKSPMAgtfyrspapgeppfvKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEI 255
|
90
....*....|....*
gi 15231159 143 LVTEGsKDIPVNEPI 157
Cdd:PLN02983 256 LAEDG-KPVSVDTPL 269
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
131-287 |
6.91e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.44 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231159 131 FESQEEGFLAKILVTEGSKDIPVNE-PIAIMVEEEDDIKNVPatIEGGRDGKEETSAHQVMKPDESTQQKSSIQPDASDL 209
Cdd:PRK09282 439 LEEREAGELKPEPEPKEAAAAGAEGiPTEFKVEVDGEKYEVK--IEGVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGR 516
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231159 210 PPHVVLEmpALSPTMnQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGsKDVAVGKPIALI 287
Cdd:PRK09282 517 PRASAPG--AVTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG-DRVNPGDVLMEI 590
|
|
| |
