|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
79-492 |
1.83e-154 |
|
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: 446.93 E-value: 1.83e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 79 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 158
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 159 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 214
Cdd:TIGR01349 81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 215 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 292
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 293 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 370
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 371 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 450
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2756270947 451 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 492
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
70-488 |
9.49e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 413.48 E-value: 9.49e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 70 SSTGFPPHLVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPI 149
Cdd:PLN02744 105 SSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 150 AVTVEDLEDI---KNIPADASFGG---------------EQKEQSIASEAQKVETDAAKESSIITRISPAAKLLIKEHRL 211
Cdd:PLN02744 185 AITVEEEEDIgkfKDYKPSSSAAPaapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 212 DQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPSSQpthdfqaqsvtipqqndaYEDIPNSQIRKVIAKRLL 291
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALD------------------YTDIPNTQIRKVTASRLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 292 ESKQTTPHLYLSQDVILDPLLAFRNEL----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISI 367
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLnslqEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH--NVNINV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 368 AVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNL-GMYPVDHFCAIINPPQSGILAVGR 446
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGS 484
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2756270947 447 GNKiiePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKF 488
Cdd:PLN02744 485 AEK---RVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
290-492 |
1.04e-83 |
|
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: 257.86 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 290 LLESKQTTPHLYLSQDVILDPLLAFRNELKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDIS 366
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 367 IAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGR 446
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2756270947 447 GNKiiEPVVDSDGTEKATVvtkMSLTLSADHRVFDGQVGGKFFTEL 492
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKV---MPLSLSFDHRVIDGAEAARFLNTL 201
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
82-151 |
9.75e-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: 105.56 E-value: 9.75e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 82 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 151
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
82-151 |
2.27e-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: 98.99 E-value: 2.27e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 82 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 151
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
79-492 |
1.83e-154 |
|
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: 446.93 E-value: 1.83e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 79 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 158
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 159 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 214
Cdd:TIGR01349 81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 215 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 292
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 293 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 370
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 371 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 450
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2756270947 451 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 492
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
70-488 |
9.49e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 413.48 E-value: 9.49e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 70 SSTGFPPHLVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPI 149
Cdd:PLN02744 105 SSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 150 AVTVEDLEDI---KNIPADASFGG---------------EQKEQSIASEAQKVETDAAKESSIITRISPAAKLLIKEHRL 211
Cdd:PLN02744 185 AITVEEEEDIgkfKDYKPSSSAAPaapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 212 DQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPSSQpthdfqaqsvtipqqndaYEDIPNSQIRKVIAKRLL 291
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALD------------------YTDIPNTQIRKVTASRLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 292 ESKQTTPHLYLSQDVILDPLLAFRNEL----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISI 367
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLnslqEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH--NVNINV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 368 AVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNL-GMYPVDHFCAIINPPQSGILAVGR 446
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGS 484
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2756270947 447 GNKiiePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKF 488
Cdd:PLN02744 485 AEK---RVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
82-492 |
1.37e-137 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 403.02 E-value: 1.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 82 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDIKN 161
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAV-IEEEGEAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 162 IPADASFGGEQKEQSIASEAQKVETDAA------KESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALK 235
Cdd:PRK11856 85 AAAAEAAPEAPAPEPAPAAAAAAAAAPAaaaapaAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 236 LGASSSSTKQKNAPAAPSSQPthdfqaqsvtipqqnDAYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR 315
Cdd:PRK11856 165 AAAPAAAAAAAAAAAPPAAAA---------------EGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 316 NELKEQhGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTPIIRNADQKTISAISSEV 395
Cdd:PRK11856 230 KQLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKK--YVNIGIAVATDGGLIVPVIRDADKKSLFELAREI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 396 KQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRgnkIIEPVVDSDGteKATVVTKMSLTLSA 475
Cdd:PRK11856 307 KDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGA---IVERPVVVDG--EIVVRKVMPLSLSF 381
|
410
....*....|....*..
gi 2756270947 476 DHRVFDGQVGGKFFTEL 492
Cdd:PRK11856 382 DHRVIDGADAARFLKAL 398
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
290-492 |
1.04e-83 |
|
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: 257.86 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 290 LLESKQTTPHLYLSQDVILDPLLAFRNELKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDIS 366
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 367 IAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGR 446
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2756270947 447 GNKiiEPVVDSDGTEKATVvtkMSLTLSADHRVFDGQVGGKFFTEL 492
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKV---MPLSLSFDHRVIDGAEAARFLNTL 201
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
83-504 |
1.14e-82 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 262.08 E-value: 1.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 83 PALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAVTVEDLEDIKNI 162
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAAAGAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 163 PADASfggeqKEQSIASEAQKVETDAAKESSIItrISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALklgASSSS 242
Cdd:PRK05704 87 AAAAA-----AAAAAAAPAQAQAAAAAEQSNDA--LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAAL---AAAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 243 TKQKNAPAAPSSQPTHDFqAQSVtipqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELKEQ- 321
Cdd:PRK05704 157 APAAPAAAAPAAAPAPLG-ARPE---------ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAf 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 322 ---HGVKVSVNDIVIKAVALALRNVPEANAYWNND----KEQaqkcvsVDISIAVATEKGLMTPIIRNADQKTISAISSE 394
Cdd:PRK05704 227 ekkHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDdivyHNY------YDIGIAVGTPRGLVVPVLRDADQLSFAEIEKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 395 VKQLAEKARAGKLAPNEFQGGTFSISNLGMY------PvdhfcaIINPPQSGILAVgrgNKIIE-PVVdsdgtEKATVVT 467
Cdd:PRK05704 301 IAELAKKARDGKLSIEELTGGTFTITNGGVFgslmstP------IINPPQSAILGM---HKIKErPVA-----VNGQIVI 366
|
410 420 430
....*....|....*....|....*....|....*....
gi 2756270947 468 K--MSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:PRK05704 367 RpmMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
80-504 |
2.98e-82 |
|
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: 260.82 E-value: 2.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 80 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDI 159
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI-LEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 160 KNIPADASfgGEQKEQSIASEAQKVETDAAKESSIitriSPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGAS 239
Cdd:TIGR01347 81 TAAPPAKS--GEEKEETPAASAAAAPTAAANRPSL----SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPAS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 240 SSstkqknAPAAPSSQPTHDFQAQSVtipqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELK 319
Cdd:TIGR01347 155 AQ------PPAAAAAAAAPAAATRPE---------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 320 EQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTPIIRNADQKTISAISSEV 395
Cdd:TIGR01347 220 EEfekkHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKD--YYDISVAVSTDRGLVVPVVRNADRMSFADIEKEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 396 KQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVgrgNKIIE-PVVDSDGTEkatVVTKMSLTLS 474
Cdd:TIGR01347 298 ADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGM---HGIKErPVAVNGQIE---IRPMMYLALS 371
|
410 420 430
....*....|....*....|....*....|
gi 2756270947 475 ADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
92-504 |
1.63e-78 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 255.52 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 92 GNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDIKNIPADASFGGE 171
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV-IEVAAAAPAAAAAPAAAAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 172 QKEQSIASEA--------QKVETDAAKESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGASSSST 243
Cdd:PRK11855 211 AAAAAAAPAPapaaaaapAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 244 KQKNAPAAPS------SQPTHDFqAQSVTIpqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 317
Cdd:PRK11855 291 AAAAAAAAGGgglgllPWPKVDF-SKFGEI-------ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 318 LKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNND-KEQAQKcVSVDISIAVATEKGLMTPIIRNADQKTISAISS 393
Cdd:PRK11855 363 LKKEAekaGVKLTMLPFFIKAVVAALKEFPVFNASLDEDgDELTYK-KYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAR 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 394 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGnkIIEPVvdSDGTEkatVVTK--MSL 471
Cdd:PRK11855 442 EIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKS--QMKPV--WDGKE---FVPRlmLPL 514
|
410 420 430
....*....|....*....|....*....|...
gi 2756270947 472 TLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:PRK11855 515 SLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
80-504 |
8.08e-66 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 224.11 E-value: 8.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 80 VGMPALSPTmnQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtvedLEDI 159
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMR----FEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 160 KNIPADASfGGEQKEQSIASEAQKVETDAA-----------KESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKG 228
Cdd:PRK11854 282 GAAPAAAP-AKQEAAAPAPAAAKAEAPAAApaakaegksefAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 229 DVLAALKlgasSSSTKQKNAPAAPSSQ---------PTHDFQAQSVTipqqndayEDIPNSQIRKVIAKRLLESKQTTPH 299
Cdd:PRK11854 361 DVQAYVK----DAVKRAEAAPAAAAAGgggpgllpwPKVDFSKFGEI--------EEVELGRIQKISGANLHRNWVMIPH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 300 LYLSQDVILDPLLAFRNE-----LKEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKG 374
Cdd:PRK11854 429 VTQFDKADITELEAFRKQqnaeaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 375 LMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKiiEPV 454
Cdd:PRK11854 509 LVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAM--EPV 586
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2756270947 455 VDSdgteKATVVTKM-SLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:PRK11854 587 WNG----KEFAPRLMlPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
78-504 |
3.68e-59 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 201.06 E-value: 3.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 78 LVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAVtvedle 157
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSE------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 158 dIKNIPADASFGGEQKEQSIASEAQKVETDAAKESSiitrisPAAKllikehrldqsvlnasgprgtllkgdvlaalklg 237
Cdd:PTZ00144 118 -IDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTP------EPPA---------------------------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 238 ASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 317
Cdd:PTZ00144 157 ASKPTPPAAAKPPEPAPAAKPPPTPVARADPRE----TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 318 LKEQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNNDkeqaqkCVS----VDISIAVATEKGLMTPIIRNADQKTIS 389
Cdd:PTZ00144 233 YKDDfqkkHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD------EIVyrnyVDISVAVATPTGLVVPVIRNCENKSFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 390 AISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGIL--------AVGRGNKI-IEPVvdsdgt 460
Cdd:PTZ00144 307 EIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhaikkrPVVVGNEIvIRPI------ 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2756270947 461 ekatvvtkMSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:PTZ00144 381 --------MYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
102-504 |
5.38e-53 |
|
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: 187.77 E-value: 5.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 102 GEKIEVGDVICEIETDKATLEF----------------ESLEEGYLAKILAPEGSKDVQVGQPIAVTvedledikniPAD 165
Cdd:TIGR01348 140 GDTVSADQSLITLESDKASMEVpapasgvvksvkvkvgDSVPTGDLILTLSVAGSTPATAPAPASAQ----------PAA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 166 ASFGGEQKEQSIASEAQKVETDAAKES-----SIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKlgass 240
Cdd:TIGR01348 210 QSPAATQPEPAAAPAAAKAQAPAPQQAgtqnpAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK----- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 241 ssTKQKNAPAAPSSqpTHDFQAQSVTIPQQN----DAYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR- 315
Cdd:TIGR01348 285 --EPSVRAQAAAAS--AAGGAPGALPWPNVDfskfGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRk 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 316 --NELKEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISS 393
Cdd:TIGR01348 361 qqNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELAL 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 394 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGnkIIEPVvdSDGTEKATVVTkMSLTL 473
Cdd:TIGR01348 441 ELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKS--GMEPV--WNGKEFEPRLM-LPLSL 515
|
410 420 430
....*....|....*....|....*....|.
gi 2756270947 474 SADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:TIGR01348 516 SYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
158-494 |
1.29e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 181.64 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 158 DIKNIPADASFGGEQKEQsiaseaqkVETdaAKESSIItRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALklg 237
Cdd:PRK14843 22 NLYDVSGSGANGRVHKED--------VET--YKDTNVV-RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 238 asssSTKQKNAPAAPSSQPTHDFQAQSVTIPQQNdaYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 317
Cdd:PRK14843 88 ----PENIENDSIKSPAQIEKVEEVPDNVTPYGE--IERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 318 L----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISS 393
Cdd:PRK14843 162 VlepiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 394 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVgrGNKIIEPVVDSDgteKATVVTKMSLTL 473
Cdd:PRK14843 242 AFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV--SSTIEKPVVVNG---EIVIRPIMSLGL 316
|
330 340
....*....|....*....|.
gi 2756270947 474 SADHRVFDGQVGGKFFTELSQ 494
Cdd:PRK14843 317 TIDHRVVDGMAGAKFMKDLKE 337
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
96-504 |
1.42e-47 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 169.90 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 96 KWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQP-IAVTVEDLEDIKNIPADASFGGEqKE 174
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETlLKIMVEDSQHLRSDSLLLPTDSS-NI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 175 QSIASEAQKVETdaakESSIITriSPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVL--AALKLGASSSSTKQKNAPAAP 252
Cdd:PLN02528 95 VSLAESDERGSN----LSGVLS--TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLkyAAQKGVVKDSSSAEEATIAEQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 253 SSQPTHdfqaqSVTIPQQNDAYEDIPNSQIRKVIAKRLLESKQTtPHLYLSQDVILDPLLAFR---NELKEQHGVKVSVN 329
Cdd:PLN02528 169 EEFSTS-----VSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKV-PHFHYVEEINVDALVELKasfQENNTDPTVKHTFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 330 DIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAP 409
Cdd:PLN02528 243 PFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 410 NEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKIiePVVDSDGTEKATVVtkMSLTLSADHRVFDGQVGGKFF 489
Cdd:PLN02528 323 EDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKV--PRFVDDGNVYPASI--MTVTIGADHRVLDGATVARFC 398
|
410
....*....|....*
gi 2756270947 490 TELSQNFGDIRRLLL 504
Cdd:PLN02528 399 NEWKSYVEKPELLML 413
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
80-490 |
1.74e-42 |
|
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: 159.41 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 80 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEgSKDVQVGQPIAVTVEDLED- 158
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPGEAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 159 ---------------------------------------------------------------IKNI------------- 162
Cdd:TIGR02927 84 sepapaapepeaapepeapapaptpaaeapapaapqaggsgeatevkmpelgesvtegtvtswLKAVgdtvevdepllev 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 163 ----------------------------------------------------PADASFGGEQKEQSIASEAQKVETDAAK 190
Cdd:TIGR02927 164 stdkvdteipspvagtlleirapeddtvevgtvlaiigdanaapaepaeeeaPAPSEAGSEPAPDPAARAPHAAPDPPAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 191 -----------------ESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPS 253
Cdd:TIGR02927 244 apapaktaapaaaapvsSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 254 SQPTHDFQAQSVTIPQQNDAYEDIpnSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR----NELKEQHGVKVSVN 329
Cdd:TIGR02927 324 AAPAAAAKPAEPDTAKLRGTTQKM--NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRarakNDFLEKNGVNLTFL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 330 DIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAP 409
Cdd:TIGR02927 402 PFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 410 NEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKIIEPVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFF 489
Cdd:TIGR02927 482 DELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFL 561
|
.
gi 2756270947 490 T 490
Cdd:TIGR02927 562 T 562
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
67-504 |
1.38e-41 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 154.91 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 67 RWL----SSTGFPPHLVVgmPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKd 142
Cdd:PLN02226 79 RWVrpfsSESGDTVEAVV--PHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDT- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 143 VQVGQPIAVTvedlediknipadasfggeqkeqsiaseaqkvetdaAKESSIITRISPAAKLlikehrldqsvlnasgPR 222
Cdd:PLN02226 156 VEPGTKVAII------------------------------------SKSEDAASQVTPSQKI----------------PE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 223 GTLLKGDVLAALKLGASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQnDAYEDIPNSQIRKVIAKRLLESKQTTPHLYL 302
Cdd:PLN02226 184 TTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLPPK-ERERRVPMTRLRKRVATRLKDSQNTFALLTT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 303 SQDVILDPLLAFRNELK----EQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTP 378
Cdd:PLN02226 263 FNEVDMTNLMKLRSQYKdafyEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRD--YVDISIAVGTSKGLVVP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 379 IIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILavGRGNKIIEPVVDSd 458
Cdd:PLN02226 341 VIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAIL--GMHSIVSRPMVVG- 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2756270947 459 gtekATVVTK--MSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 504
Cdd:PLN02226 418 ----GSVVPRpmMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
198-494 |
9.56e-38 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 140.31 E-value: 9.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 198 ISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLaalKLGASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQNDAYEDi 277
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVE---NFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 278 PNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELKEQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNND 353
Cdd:PRK11857 80 KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlktEGVKLTFLPFIAKAILIALKEFPIFAAKYDEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 354 KEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAI 433
Cdd:PRK11857 160 TSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2756270947 434 INPPQSGILAVGrgnKIIEPVVDSDGTEKATVVtkMSLTLSADHRVFDGQVGGKFFTELSQ 494
Cdd:PRK11857 240 INYPELAIAGVG---AIIDKAIVKNGQIVAGKV--MHLTVAADHRWIDGATIGRFASRVKE 295
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
82-194 |
1.54e-35 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 138.13 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 82 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLEDIKN 161
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
90 100 110
....*....|....*....|....*....|...
gi 2756270947 162 IPADASFGGEQKEQSIASEAQKVETDAAKESSI 194
Cdd:PRK11892 87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
82-151 |
9.75e-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: 105.56 E-value: 9.75e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 82 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 151
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
82-151 |
2.27e-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: 98.99 E-value: 2.27e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 82 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 151
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
80-188 |
1.79e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.76 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 80 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAV----TVED 155
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVvadaEVSD 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 2756270947 156 LED---IKNIPADASFGGEQkEQSIASEAQKVETDA 188
Cdd:PRK14875 84 AEIdafIAPFARRFAPEGID-EEDAGPAPRKARIGG 118
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
79-151 |
2.66e-16 |
|
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: 73.40 E-value: 2.66e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2756270947 79 VVGMPALSPTMNQGnIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 151
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
80-149 |
1.49e-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: 1.49e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 80 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPI 149
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPL 70
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
316-494 |
8.04e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 61.44 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 316 NELKEQHGVKVSVNDIVIKAVALALRNVPEANAYWN--NDKEQAQKCVSVDISIAVATEK-----GLMTPIIRNADQKTI 388
Cdd:PRK12270 160 NHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDF 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756270947 389 SAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRgnkiIEPVVDSDGTEKATV--- 465
Cdd:PRK12270 240 AQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGA----MEYPAEFQGASEERLael 315
|
170 180 190
....*....|....*....|....*....|.
gi 2756270947 466 -VTK-MSLTLSADHRVFDGQVGGKFFTELSQ 494
Cdd:PRK12270 316 gISKvMTLTSTYDHRIIQGAESGEFLRTIHQ 346
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
91-151 |
3.47e-06 |
|
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: 44.33 E-value: 3.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2756270947 91 QGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 151
Cdd:cd06850 7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVV 66
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
197-231 |
1.27e-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: 41.90 E-value: 1.27e-05
10 20 30
....*....|....*....|....*....|....*
gi 2756270947 197 RISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVL 231
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| |
