|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
290-713 |
3.69e-146 |
|
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: 433.45 E-value: 3.69e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 290 VLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAES 369
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 370 IEAIKS----------------------SSAGSSEVDTVKEVPDSVVDKPTERKAGFTKI--SPAAKLLILEHGLEASSI 425
Cdd:TIGR01349 81 VADAFKnyklessaspapkpseiaptapPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIfaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 426 EASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSSTSKPSVTQSDN-NYEDFPNSQIRKIIAKRLLESKQ 504
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSP-----------ASANQQAAATTPATYPAAAPVSTgSYEDVPLSNIRKIIAKRLLESKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 505 KIPHLYLQSDVVLDPLLAFRKELQE--NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEK 582
Cdd:TIGR01349 230 TIPHYYVSIECNVDKLLALRKELNAmaSEVYKLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 583 GLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVvep 662
Cdd:TIGR01349 308 GLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV--- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 334185925 663 VIGLDGIEKP-SVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:TIGR01349 385 AVVDNDEEKGfAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
293-713 |
8.42e-134 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 400.71 E-value: 8.42e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 293 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIVEDAESIEA 372
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEAEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 373 IKSSSAGSSEVDTVKEVPDSVVDKPTER-------KAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIas 445
Cdd:PRK11856 86 AAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 446 gkaskssastkkkQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK 525
Cdd:PRK11856 164 -------------AAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 526 ELQENhGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVK 605
Cdd:PRK11856 231 QLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 606 ELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGnkVVEPVIGlDGieKPSVVTKMNVTLSAD 685
Cdd:PRK11856 308 DLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI--VERPVVV-DG--EIVVRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 334185925 686 HRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
499-712 |
2.81e-81 |
|
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: 257.09 E-value: 2.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 499 LLESKQKIPHLYLQSDVVLDPLLAFRKELQENH---GVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDIS 575
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 576 IAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGR 655
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185925 656 GNKVvePVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLL 712
Cdd:pfam00198 161 IRKR--PVVVDGEIV---VRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
166-249 |
6.17e-32 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 129.65 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKN 245
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
....
gi 334185925 246 VPAT 249
Cdd:PRK11892 87 AGAA 90
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
166-236 |
4.42e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.49 E-value: 4.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 236
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
289-363 |
6.27e-26 |
|
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: 101.33 E-value: 6.27e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185925 289 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 363
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
166-237 |
3.03e-25 |
|
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: 99.37 E-value: 3.03e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIMV 237
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
289-364 |
3.14e-23 |
|
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: 93.59 E-value: 3.14e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185925 289 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIV 364
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
162-236 |
1.03e-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: 72.25 E-value: 1.03e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185925 162 TVLAMPALSPTMsHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 236
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 ... |
290-713 |
3.69e-146 |
|
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: 433.45 E-value: 3.69e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 290 VLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAES 369
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 370 IEAIKS----------------------SSAGSSEVDTVKEVPDSVVDKPTERKAGFTKI--SPAAKLLILEHGLEASSI 425
Cdd:TIGR01349 81 VADAFKnyklessaspapkpseiaptapPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIfaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 426 EASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSSTSKPSVTQSDN-NYEDFPNSQIRKIIAKRLLESKQ 504
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSP-----------ASANQQAAATTPATYPAAAPVSTgSYEDVPLSNIRKIIAKRLLESKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 505 KIPHLYLQSDVVLDPLLAFRKELQE--NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEK 582
Cdd:TIGR01349 230 TIPHYYVSIECNVDKLLALRKELNAmaSEVYKLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 583 GLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVvep 662
Cdd:TIGR01349 308 GLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV--- 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 334185925 663 VIGLDGIEKP-SVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:TIGR01349 385 AVVDNDEEKGfAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
293-713 |
8.42e-134 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 400.71 E-value: 8.42e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 293 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIVEDAESIEA 372
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEAEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 373 IKSSSAGSSEVDTVKEVPDSVVDKPTER-------KAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIas 445
Cdd:PRK11856 86 AAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 446 gkaskssastkkkQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK 525
Cdd:PRK11856 164 -------------AAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 526 ELQENhGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVK 605
Cdd:PRK11856 231 QLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 606 ELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGnkVVEPVIGlDGieKPSVVTKMNVTLSAD 685
Cdd:PRK11856 308 DLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI--VERPVVV-DG--EIVVRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 334185925 686 HRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
283-713 |
7.14e-129 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 392.68 E-value: 7.14e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 283 SDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIAL 362
Cdd:PLN02744 107 SDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 363 IVEDAESIEAIK----SSSAGSS--------------EVDTVKEVPDSVVDKPTERKAGFTKI--SPAAKLLILEHGLEA 422
Cdd:PLN02744 187 TVEEEEDIGKFKdykpSSSAAPAapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIfaSPLARKLAEDNNVPL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 423 SSIEASGPYGTLLKSDVVAAIasgkaskssastkkKQPSKETPSKSSSTSKPsvtqSDNNYEDFPNSQIRKIIAKRLLES 502
Cdd:PLN02744 267 SSIKGTGPDGRIVKADIEDYL--------------ASGGKGATAPPSTDSKA----PALDYTDIPNTQIRKVTASRLLQS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 503 KQKIPHLYLQSDVVLDPLLAFRKEL---QENHGVK-VSVNDIVIKAVAVALRNVRQANAFWDAEKgdIVMCDSVDISIAV 578
Cdd:PLN02744 329 KQTIPHYYLTVDTRVDKLMALRSQLnslQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTDDY--IRQYHNVNINVAV 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 579 ATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNL-GMYPVDNFCAIINPPQAGILAVGRGN 657
Cdd:PLN02744 407 QTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAE 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185925 658 KVVEPVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:PLN02744 487 KRVIPGSGPDQYN---FASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
176-713 |
6.12e-88 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 286.33 E-value: 6.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 176 GNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM-VEEEDDIKNVPATIEggr 254
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGLLAVIeAAGAAAAAAAPAAAA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 255 dgKEETSAHQVMKPDESTQQKSSIQPDASDLPphvvLEMPALSpTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEF 334
Cdd:PRK11855 92 --APAAAAAAAPAPAAAAPAAAAAAAGGGVVE----VKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 335 ESLEEGYLAKILIPEGSKdVAVGKPIALIvEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKI------- 407
Cdd:PRK11855 165 PSPVAGVVKEIKVKVGDK-VSVGSLLVVI-EVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAaaapgka 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 408 ---SPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSSTSKPSVTQSDNNYE 484
Cdd:PRK11855 243 phaSPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAM-----------SAAAAAAAAAAAAGGGGLGLLPWPKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 485 DF---------PNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQ---ENHGVKVSVNDIVIKAVAVALRNV 552
Cdd:PRK11855 312 DFskfgeietkPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKkeaEKAGVKLTMLPFFIKAVVAALKEF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 553 RQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLG 632
Cdd:PRK11855 392 PVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 633 MYPVDNFCAIINPPQAGILAVGRGnkVVEPVigldgIEKPSVVTK--MNVTLSADHRIFDGQVGASFMSELRSNFEDVRR 710
Cdd:PRK11855 472 GIGGTAFTPIINAPEVAILGVGKS--QMKPV-----WDGKEFVPRlmLPLSLSYDHRVIDGATAARFTNYLKQLLADPRR 544
|
...
gi 334185925 711 LLL 713
Cdd:PRK11855 545 MLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
499-712 |
2.81e-81 |
|
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: 257.09 E-value: 2.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 499 LLESKQKIPHLYLQSDVVLDPLLAFRKELQENH---GVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDIS 575
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 576 IAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGR 655
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334185925 656 GNKVvePVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLL 712
Cdd:pfam00198 161 IRKR--PVVVDGEIV---VRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
294-713 |
2.79e-73 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 243.20 E-value: 2.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 294 PALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSkDVAVGKPIALIVEDAESieAI 373
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAAA--GA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 374 KSSSAGSSEVDTVKEVPDSVVDKPTERKAGftkISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGkaskssa 453
Cdd:PRK05704 85 AAAAAAAAAAAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAA------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 454 stkkkqPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQE---- 529
Cdd:PRK05704 155 ------AAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDafek 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 530 NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEkgDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQ 609
Cdd:PRK05704 229 KHGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 610 KARSGKLAPHEFQGGTFSISNLGMY------PvdnfcaIINPPQAGILAVgrgNKVVEPVIGLDGiekpSVVTK--MNVT 681
Cdd:PRK05704 307 KARDGKLSIEELTGGTFTITNGGVFgslmstP------IINPPQSAILGM---HKIKERPVAVNG----QIVIRpmMYLA 373
|
410 420 430
....*....|....*....|....*....|..
gi 334185925 682 LSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:PRK05704 374 LSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
176-713 |
1.67e-69 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 239.52 E-value: 1.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 176 GNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdipVNEPIAIMVEEeddiknvpatieggrD 255
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK---VSTGSLIMVFE---------------V 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 256 GKEETSAhqvmKPDESTQQKSSIQPDASDLPPHVvlEMPALSPTmnQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFE 335
Cdd:PRK11854 180 AGEAPAA----APAAAEAAAPAAAPAAAAGVKDV--NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 336 SLEEGYLAKILIPEGSKdVAVGKPIAlIVEDAESIEAIKSSSAGSSE---VDTVKEVPDSVVDKPTERKAGFTK------ 406
Cdd:PRK11854 252 APFAGTVKEIKVNVGDK-VKTGSLIM-RFEVEGAAPAAAPAKQEAAApapAAAKAEAPAAAPAAKAEGKSEFAEndayvh 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 407 ISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKaskssastkkkqPSKETPSKSSSTSKPSVTQSDNNYEDF 486
Cdd:PRK11854 330 ATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAV------------KRAEAAPAAAAAGGGGPGLLPWPKVDF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 487 ---------PNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKE-----LQENHGVKVSVNDIVIKAVAVALRNV 552
Cdd:PRK11854 398 skfgeieevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQqnaeaEKRKLGVKITPLVFIMKAVAAALEQM 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 553 RQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLG 632
Cdd:PRK11854 478 PRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIG 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 633 MYPVDNFCAIINPPQAGILAVGRgnKVVEPVIGLDGIEkpsVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLL 712
Cdd:PRK11854 558 GLGTTHFTPIVNAPEVAILGVSK--SAMEPVWNGKEFA---PRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLV 632
|
.
gi 334185925 713 L 713
Cdd:PRK11854 633 L 633
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
291-713 |
2.25e-69 |
|
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: 232.70 E-value: 2.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 291 LEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIVEDAESI 370
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 371 EAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAgftkiSPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAiasgkask 450
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAASAAAAPTAAANRPSL-----SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 451 sSASTKKKQPSKETPSKSSSTskpsvtQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQE- 529
Cdd:TIGR01347 149 -TEAPASAQPPAAAAAAAAPA------AATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEe 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 530 ---NHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEkgDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKE 606
Cdd:TIGR01347 222 fekKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIAD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 607 LAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILavgrgnkvvepviGLDGI-EKPSVVTK-------M 678
Cdd:TIGR01347 300 LGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAIL-------------GMHGIkERPVAVNGqieirpmM 366
|
410 420 430
....*....|....*....|....*....|....*
gi 334185925 679 NVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:TIGR01347 367 YLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
166-707 |
4.12e-68 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 234.14 E-value: 4.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEgSKDIPVNEPIAIMVEE-EDDIK 244
Cdd:TIGR02927 7 MPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPgEAGSE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 245 NVPATIEGGRDGKEETSAHQVmKPDESTQQKSSIQPDASDLPPHVvlEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGE 324
Cdd:TIGR02927 86 PAPAAPEPEAAPEPEAPAPAP-TPAAEAPAPAAPQAGGSGEATEV--KMPELGESVTEGTVTSWLKAVGDTVEVDEPLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 325 IETDKATLEFESLEEGYLAKILIPEgSKDVAVGKPIALI------VEDAESIEAIKSSSAGSSEV-----DTVKEVPDSV 393
Cdd:TIGR02927 163 VSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIgdanaaPAEPAEEEAPAPSEAGSEPApdpaaRAPHAAPDPP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 394 VDKPTERK-------------AGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAiaSGKASKSSASTKKKQP 460
Cdd:TIGR02927 242 APAPAPAKtaapaaaapvssgDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAA--AKAAEEARAAAAAPAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 461 SKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK----ELQENHGVKVS 536
Cdd:TIGR02927 320 AAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRAraknDFLEKNGVNLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 537 VNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKL 616
Cdd:TIGR02927 400 FLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 617 APHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVVEPVIGLDGIEKPSVVTKMNVTLSADHRIFDGQVGAS 696
Cdd:TIGR02927 480 KPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGR 559
|
570
....*....|.
gi 334185925 697 FMSELRSNFED 707
Cdd:TIGR02927 560 FLTTIKKRLEE 570
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
174-713 |
5.19e-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: 211.27 E-value: 5.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 174 SHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIMVEEEDDIKNVPATIEGG 253
Cdd:TIGR01348 12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDT-LPVGGVIATLEVGAGAQAQAEAKKEAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 254 ---RDGKEETSAHQVMKPDEStqQKSSIQ----PDASDLPPHVVLEMPAlsptmnqgniakwwkKEGDKIEVGDVIGEIE 326
Cdd:TIGR01348 91 papTAGAPAPAAQAQAAPAAG--QSSGVQevtvPDIGDIEKVTVIEVLV---------------KVGDTVSADQSLITLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 327 TDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIaLIVEDAESIEAI-----KSSSAGSSEVDTVKEVP----------D 391
Cdd:TIGR01348 154 SDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLI-LTLSVAGSTPATapapaSAQPAAQSPAATQPEPAaapaaakaqaP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 392 SVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKaskssastkkkQPSKETPSKSSST 471
Cdd:TIGR01348 232 APQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPS-----------VRAQAAAASAAGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 472 SKPSVTQSDNNYEDF------PNSQIRKIIAKRLLESKQKIPHL--YLQSDVVldPLLAFRKELQ---ENHGVKVSVNDI 540
Cdd:TIGR01348 301 APGALPWPNVDFSKFgeveevDMSRIRKISGANLTRNWTMIPHVthFDKADIT--EMEAFRKQQNaavEKEGVKLTVLHI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 541 VIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHE 620
Cdd:TIGR01348 379 LMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 621 FQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGnkVVEPVigLDGIE-KPSVVtkMNVTLSADHRIFDGQVGASFMS 699
Cdd:TIGR01348 459 MQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKS--GMEPV--WNGKEfEPRLM--LPLSLSYDHRVIDGADAARFTT 532
|
570
....*....|....
gi 334185925 700 ELRSNFEDVRRLLL 713
Cdd:TIGR01348 533 YICESLADIRRLLL 546
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
289-713 |
9.71e-56 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 196.06 E-value: 9.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 289 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSkDVAVGKPIalivedae 368
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPL-------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 369 sieaiksssagsSEVDTVKEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASgpygtllksdvvaaiasgka 448
Cdd:PTZ00144 116 ------------SEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPP-------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 449 skssastkkKQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQ 528
Cdd:PTZ00144 164 ---------AAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 529 EN----HGVKVSVNDIVIKAVAVALRNVRQANAFWDaeKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEV 604
Cdd:PTZ00144 235 DDfqkkHGVKLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 605 KELAQKARSGKLAPHEFQGGTFSISNLGMY------PvdnfcaIINPPQAGIL--------AVGRGNKVV-EPVigldgi 669
Cdd:PTZ00144 313 ADLAEKARNNKLTLEDMTGGTFTISNGGVFgslmgtP------IINPPQSAILgmhaikkrPVVVGNEIViRPI------ 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 334185925 670 ekpsvvtkMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:PTZ00144 381 --------MYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
307-713 |
6.00e-48 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 174.52 E-value: 6.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 307 KWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKP-IALIVED--AESIEAIKSSSAGSsev 383
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETlLKIMVEDsqHLRSDSLLLPTDSS--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 384 dtvkEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKE 463
Cdd:PLN02528 93 ----NIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSAEEATIAEQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 464 TPSKSSSTskpsvTQSDNNYED--FPNSQIRKIIAKRLLESKQkIPHLYLQSDVVLDPLLAFRKELQEN---HGVKVSVN 538
Cdd:PLN02528 169 EEFSTSVS-----TPTEQSYEDktIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQENntdPTVKHTFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 539 DIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAP 618
Cdd:PLN02528 243 PFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 619 HEFQGGTFSISNLG------MYPVdnfcaiINPPQAGILAVGRGNKVVEPVIglDGIEKPSVVtkMNVTLSADHRIFDGQ 692
Cdd:PLN02528 323 EDITGGTITLSNIGaiggkfGSPV------LNLPEVAIIALGRIQKVPRFVD--DGNVYPASI--MTVTIGADHRVLDGA 392
|
410 420
....*....|....*....|.
gi 334185925 693 VGASFMSELRSNFEDVRRLLL 713
Cdd:PLN02528 393 TVARFCNEWKSYVEKPELLML 413
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
406-713 |
9.71e-47 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 169.32 E-value: 9.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 406 KISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIAsgkaskssastkkkqPSKETPSKSSSTSKPSVTQSDNN--- 482
Cdd:PRK14843 50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLP---------------ENIENDSIKSPAQIEKVEEVPDNvtp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 483 ---YEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKEL----QENHGVKVSVNDIVIKAVAVALRNVRQA 555
Cdd:PRK14843 115 ygeIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVlepiMEATGKKTTVTDLLSLAVVKTLMKHPYI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 556 NAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYP 635
Cdd:PRK14843 195 NASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 636 VDNFCAIINPPQAGILAVGrgnkvvepviglDGIEKPSVVTK-------MNVTLSADHRIFDGQVGASFMSELRSNFEDV 708
Cdd:PRK14843 275 VQSFGPIINQPNSAILGVS------------STIEKPVVVNGeivirpiMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
....*
gi 334185925 709 RRLLL 713
Cdd:PRK14843 343 ISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
270-713 |
3.67e-42 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 159.54 E-value: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 270 ESTQQKSSIQPDASDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPE 349
Cdd:PLN02226 73 VSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 350 GSKdvavgkpialiVEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPterkagftkiSPAAKllilehgleassieasg 429
Cdd:PLN02226 153 GDT-----------VEPGTKVAIISKSEDAASQVTPSQKIPETTDPKP----------SPPAE----------------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 430 pygTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSkssstskpsvtQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHL 509
Cdd:PLN02226 195 ---DKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQL-----------PPKERERRVPMTRLRKRVATRLKDSQNTFALL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 510 YLQSDVVLDPLLAFRKELQ----ENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEkgDIVMCDSVDISIAVATEKGLM 585
Cdd:PLN02226 261 TTFNEVDMTNLMKLRSQYKdafyEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 586 TPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILavGRGNKVVEP-VI 664
Cdd:PLN02226 339 VPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAIL--GMHSIVSRPmVV 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 334185925 665 GLDGIEKPsvvtKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL 713
Cdd:PLN02226 417 GGSVVPRP----MMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
293-412 |
4.87e-38 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 147.76 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 293 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAESIEA 372
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 334185925 373 IKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKISPAAK 412
Cdd:PRK11892 87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAE 126
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
406-706 |
3.34e-34 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 132.61 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 406 KISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSKSSSTSKPSVTQSDNNyed 485
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 486 fPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRK----ELQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDA 561
Cdd:PRK11857 80 -KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKsvkdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 562 EKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLG----MYPVd 637
Cdd:PRK11857 159 ATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGsvgsLYGV- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185925 638 nfcAIINPPQAGILAVGrgnKVVEPVIGLDGIEKPSVVtkMNVTLSADHRIFDGQVGASFMSELRSNFE 706
Cdd:PRK11857 238 ---PVINYPELAIAGVG---AIIDKAIVKNGQIVAGKV--MHLTVAADHRWIDGATIGRFASRVKELLE 298
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
166-249 |
6.17e-32 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 129.65 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKN 245
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
....
gi 334185925 246 VPAT 249
Cdd:PRK11892 87 AGAA 90
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
166-236 |
4.42e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.49 E-value: 4.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 236
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
289-363 |
6.27e-26 |
|
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: 101.33 E-value: 6.27e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185925 289 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 363
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
166-237 |
3.03e-25 |
|
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: 99.37 E-value: 3.03e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185925 166 MPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIMV 237
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
289-364 |
3.14e-23 |
|
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: 93.59 E-value: 3.14e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185925 289 VVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALIV 364
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
162-240 |
6.39e-17 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 83.07 E-value: 6.39e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185925 162 TVLAMPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSkDIPVNEPIAIMVEEE 240
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
293-373 |
4.56e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.37 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 293 MPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSkDVAVGKPIALI----VEDAE 368
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVadaeVSDAE 85
|
....*
gi 334185925 369 sIEAI 373
Cdd:PRK14875 86 -IDAF 89
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
162-225 |
5.03e-16 |
|
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: 73.24 E-value: 5.03e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185925 162 TVLAmPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSK 225
Cdd:cd06663 1 TILI-PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
162-236 |
1.03e-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: 72.25 E-value: 1.03e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185925 162 TVLAMPALSPTMsHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKdIPVNEPIAIM 236
Cdd:pfam00364 1 TEIKSPMIGESV-REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
294-352 |
3.53e-14 |
|
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: 67.85 E-value: 3.53e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 334185925 294 PALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSK 352
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
289-363 |
1.43e-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: 66.08 E-value: 1.43e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185925 289 VVLEMPALSPTMNQGnIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 363
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
176-224 |
1.49e-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: 48.95 E-value: 1.49e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 334185925 176 GNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGS 224
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
527-691 |
3.86e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 53.74 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 527 LQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGD--IVMCDSVDISIAVATEK-----GLMTPIIKNADQKSISA 599
Cdd:PRK12270 162 LKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGKptLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 600 ISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVG--------RGNKvvEPVIGLDGIEK 671
Cdd:PRK12270 242 FWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGameypaefQGAS--EERLAELGISK 319
|
170 180
....*....|....*....|
gi 334185925 672 psVVTkmnVTLSADHRIFDG 691
Cdd:PRK12270 320 --VMT---LTSTYDHRIIQG 334
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
406-439 |
4.57e-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: 40.75 E-value: 4.57e-05
10 20 30
....*....|....*....|....*....|....
gi 334185925 406 KISPAAKLLILEHGLEASSIEASGPYGTLLKSDV 439
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
168-223 |
4.83e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 46.76 E-value: 4.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 334185925 168 ALSPTMShGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEG 223
Cdd:PRK09282 524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
288-363 |
3.35e-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: 39.32 E-value: 3.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185925 288 HVVLEMPalsptmnqGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKdVAVGKPIALI 363
Cdd:cd06850 1 EVTAPMP--------GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
184-235 |
6.42e-04 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 40.26 E-value: 6.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 334185925 184 KEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSkdiPVN--EPIAI 235
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ---PVEygQPLFV 134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
207-363 |
5.80e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.83 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 207 FESQEEGFLAKILVTEGSKDIPVNE-PIAIMVEEEDDIKNVPatIEGGrdgKEETSAHQVMKPD---ESTQQKSSIQPDA 282
Cdd:PRK09282 439 LEEREAGELKPEPEPKEAAAAGAEGiPTEFKVEVDGEKYEVK--IEGV---KAEGKRPFYLRVDgmpEEVVVEPLKEIVV 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185925 283 SDLPPHVVLEmpALSPTMnQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGsKDVAVGKPIAL 362
Cdd:PRK09282 514 GGRPRASAPG--AVTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG-DRVNPGDVLME 589
|
.
gi 334185925 363 I 363
Cdd:PRK09282 590 I 590
|
|
| |
