|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
55-483 |
0e+00 |
|
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: 679.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 55 VINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVENEGD 134
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 135 VA-AMADFTIEDS-------SAKEPSAKSGEEKSAPSSEKQSKETSSPSNVSGEERGDRVFASPLARKLAEEKDLDLSQI 206
Cdd:TIGR01349 81 VAdAFKNYKLESSaspapkpSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 207 RGSGPNGRIIKVDIENFKPVvAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVS 286
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQ-SPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 287 VNMEKIIRLRAALNAMADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHA 366
Cdd:TIGR01349 240 CNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 367 LGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDSTSEKGFKVAP 446
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGFAVAS 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 19075255 447 IMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:TIGR01349 400 IMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
51-483 |
5.73e-162 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 469.33 E-value: 5.73e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 51 PAHTVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVE 130
Cdd:PLN02744 110 PPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 131 NEGDVAAMADFTiEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPS-----NVSGEERGDRVFASPLARKLAEEKDLDLSQ 205
Cdd:PLN02744 190 EEEDIGKFKDYK-PSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEpkaskPSAPPSSGDRIFASPLARKLAEDNNVPLSS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 206 IRGSGPNGRIIKVDIENF-----KPVVAPKPSNEAAAKAttpaasaadaaapgDYEDLPLSNMRKIIASRLAESKNMNPH 280
Cdd:PLN02744 269 IKGTGPDGRIVKADIEDYlasggKGATAPPSTDSKAPAL--------------DYTDIPNTQIRKVTASRLLQSKQTIPH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 281 YYVTVSVNMEKIIRLRAALNAM--ADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLIT 358
Cdd:PLN02744 335 YYLTVDTRVDKLMALRSQLNSLqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 359 PVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNL-GMFPVDQFTAIINPPQACILAVGTTVDTVVPDST 437
Cdd:PLN02744 415 PVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSG 494
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19075255 438 SEKgFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:PLN02744 495 PDQ-YNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
271-482 |
4.46e-95 |
|
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: 286.36 E-value: 4.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 271 LAESKNMNPHYYVTVSVNMEKIIRLRAALNAMADGRY-KLSVNDLVIKATTAALRQVPEVNAAWMGDF--IRQYKNVDIS 347
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 348 MAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGT 427
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19075255 428 TVDTVVPdstSEKGFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIM 482
Cdd:pfam00198 161 IRKRPVV---VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
54-127 |
1.01e-24 |
|
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: 97.09 E-value: 1.01e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075255 54 TVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAV 127
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
54-127 |
1.79e-19 |
|
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: 82.42 E-value: 1.79e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075255 54 TVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAV 127
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
55-483 |
0e+00 |
|
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: 679.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 55 VINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVENEGD 134
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 135 VA-AMADFTIEDS-------SAKEPSAKSGEEKSAPSSEKQSKETSSPSNVSGEERGDRVFASPLARKLAEEKDLDLSQI 206
Cdd:TIGR01349 81 VAdAFKNYKLESSaspapkpSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 207 RGSGPNGRIIKVDIENFKPVvAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVS 286
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQ-SPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 287 VNMEKIIRLRAALNAMADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHA 366
Cdd:TIGR01349 240 CNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 367 LGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDSTSEKGFKVAP 446
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGFAVAS 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 19075255 447 IMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:TIGR01349 400 IMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
51-483 |
5.73e-162 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 469.33 E-value: 5.73e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 51 PAHTVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVE 130
Cdd:PLN02744 110 PPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 131 NEGDVAAMADFTiEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPS-----NVSGEERGDRVFASPLARKLAEEKDLDLSQ 205
Cdd:PLN02744 190 EEEDIGKFKDYK-PSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEpkaskPSAPPSSGDRIFASPLARKLAEDNNVPLSS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 206 IRGSGPNGRIIKVDIENF-----KPVVAPKPSNEAAAKAttpaasaadaaapgDYEDLPLSNMRKIIASRLAESKNMNPH 280
Cdd:PLN02744 269 IKGTGPDGRIVKADIEDYlasggKGATAPPSTDSKAPAL--------------DYTDIPNTQIRKVTASRLLQSKQTIPH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 281 YYVTVSVNMEKIIRLRAALNAM--ADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLIT 358
Cdd:PLN02744 335 YYLTVDTRVDKLMALRSQLNSLqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 359 PVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNL-GMFPVDQFTAIINPPQACILAVGTTVDTVVPDST 437
Cdd:PLN02744 415 PVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSG 494
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19075255 438 SEKgFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:PLN02744 495 PDQ-YNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
54-483 |
7.84e-152 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 438.46 E-value: 7.84e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 54 TVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAVtVENEG 133
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAV-IEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 134 DVAAmadftiedSSAKEPSAKSGEEKSAPSSEKQSKETSSPSNVSGEERGDRVFASPLARKLAEEKDLDLSQIRGSGPNG 213
Cdd:PRK11856 81 EAEA--------AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 214 RIIKVDIENFKPVVAPKPSNEAAAKATTPAASAadaaapGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKII 293
Cdd:PRK11856 153 RITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAA------EGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 294 RLRAALNAMAdgrYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEIS 373
Cdd:PRK11856 227 ALRKQLKAIG---VKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 374 TLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDstsEKGFKVAPIMKCTLS 453
Cdd:PRK11856 304 REIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV---DGEIVVRKVMPLSLS 380
|
410 420 430
....*....|....*....|....*....|
gi 19075255 454 SDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:PRK11856 381 FDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
271-482 |
4.46e-95 |
|
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: 286.36 E-value: 4.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 271 LAESKNMNPHYYVTVSVNMEKIIRLRAALNAMADGRY-KLSVNDLVIKATTAALRQVPEVNAAWMGDF--IRQYKNVDIS 347
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 348 MAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGT 427
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19075255 428 TVDTVVPdstSEKGFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIM 482
Cdd:pfam00198 161 IRKRPVV---VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
75-483 |
2.09e-83 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 267.46 E-value: 2.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 75 KKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAVtVENEGDVAAMAdftiedsSAKEPSAK 154
Cdd:PRK11855 140 VKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV-IEVAAAAPAAA-------AAPAAAAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 155 SGEEKSAPSSEKQSKETSSPS-NVSGEERGDRVFASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENF-------KPV 226
Cdd:PRK11855 211 AAAAAAAPAPAPAAAAAPAAAaPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFvkgamsaAAA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 227 VAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRAALNAMA--D 304
Cdd:PRK11855 291 AAAAAAAAGGGGLGLLPWPKVDFSKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAekA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 305 GrYKLSVNDLVIKATTAALRQVPEVNA--AWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQR 382
Cdd:PRK11855 371 G-VKLTMLPFFIKAVVAALKEFPVFNAslDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 383 ARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVdtVVPDStSEKGFKVAPIMKCTLSSDHRVVDGA 462
Cdd:PRK11855 450 ARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQ--MKPVW-DGKEFVPRLMLPLSLSYDHRVIDGA 526
|
410 420
....*....|....*....|.
gi 19075255 463 MAARFTTALKKILENPLEIML 483
Cdd:PRK11855 527 TAARFTNYLKQLLADPRRMLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
56-483 |
8.81e-83 |
|
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: 261.59 E-value: 8.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 56 INMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAVtVENEGDV 135
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI-LEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 136 AAmadftiedssakEPSAKSGEEKSAPSSEKQSKETSSPSNvsgeergdRVFASPLARKLAEEKDLDLSQIRGSGPNGRI 215
Cdd:TIGR01347 81 TA------------APPAKSGEEKEETPAASAAAAPTAAAN--------RPSLSPAARRLAKEHGIDLSAVPGTGVTGRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 216 IKVDIENF--KPVVAPKPSNEAAAKATTPAASAAdaaapgdyEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKII 293
Cdd:TIGR01347 141 TKEDIIKKteAPASAQPPAAAAAAAAPAAATRPE--------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 294 RLRAALNA--MADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAE 371
Cdd:TIGR01347 213 ELRKRYKEefEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFAD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 372 ISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTvvPDSTSEKgFKVAPIMKCT 451
Cdd:TIGR01347 293 IEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKER--PVAVNGQ-IEIRPMMYLA 369
|
410 420 430
....*....|....*....|....*....|..
gi 19075255 452 LSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:TIGR01347 370 LSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
56-478 |
7.50e-74 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 238.58 E-value: 7.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 56 INMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTkDVPVGKPLAVTveNEGDV 135
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRI--DEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 136 AAMADftiEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPSnvsgeergdrvfasplARKLAEEKDLDLSQIRGSGPNGRI 215
Cdd:PRK05704 82 AGAAA---AAAAAAAAAAAAPAQAQAAAAAEQSNDALSPA----------------ARKLAAENGLDASAVKGTGKGGRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 216 IKVDIENFKPVVAPKPSNEAAAKATTPAASAADAAApgdyEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRL 295
Cdd:PRK05704 143 TKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPE----ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 296 RAALNAMADGRY--KLSVNDLVIKATTAALRQVPEVNAAWMGDFIrQYKN-VDISMAVATPSGLITPVIRNTHALGLAEI 372
Cdd:PRK05704 219 RKQYKDAFEKKHgvKLGFMSFFVKAVVEALKRYPEVNASIDGDDI-VYHNyYDIGIAVGTPRGLVVPVLRDADQLSFAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 373 STLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVD-TVVPDSTSEkgfkVAPIMKCT 451
Cdd:PRK05704 298 EKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKErPVAVNGQIV----IRPMMYLA 373
|
410 420
....*....|....*....|....*..
gi 19075255 452 LSSDHRVVDGAMAARFTTALKKILENP 478
Cdd:PRK05704 374 LSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
48-483 |
1.02e-72 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 235.73 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 48 KNYPAHTVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTkDVPVGKPLAV 127
Cdd:PTZ00144 39 KSYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 128 TVENEGDVAAMAdftiEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPSnvsgeergdrvfASPLARKLaeekdldlsqir 207
Cdd:PTZ00144 118 IDTGGAPPAAAP----AAAAAAKAEKTTPEKPKAAAPTPEPPAASKPT------------PPAAAKPP------------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 208 gsgpngriikvdienfKPVVAPKPSNEAAAKATTPAASaadaaapgdyedLPLSNMRKIIASRLAESKNMNPHYYVTVSV 287
Cdd:PTZ00144 170 ----------------EPAPAAKPPPTPVARADPRETR------------VPMSRMRQRIAERLKASQNTCAMLTTFNEC 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 288 NMEKIIRLRAALNAMADGRY--KLSVNDLVIKATTAALRQVPEVNAAWMGDFIrQYKN-VDISMAVATPSGLITPVIRNT 364
Cdd:PTZ00144 222 DMSALMELRKEYKDDFQKKHgvKLGFMSAFVKASTIALKKMPIVNAYIDGDEI-VYRNyVDISVAVATPTGLVVPVIRNC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 365 HALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVD--TVVPDStsekgF 442
Cdd:PTZ00144 301 ENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKrpVVVGNE-----I 375
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 19075255 443 KVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:PTZ00144 376 VIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
56-477 |
4.69e-65 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 221.41 E-value: 4.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 56 INMPALSptMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKpLAVTVENEGDV 135
Cdd:PRK11854 209 VNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 136 AAMADFTiEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPSNvsgeerGDRVFASPLARKLAEEKDLDLSQIRGSGPNGRI 215
Cdd:PRK11854 285 PAAAPAK-QEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAEN------DAYVHATPLVRRLAREFGVNLAKVKGTGRKGRI 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 216 IKVDIENF------KPVVAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNM 289
Cdd:PRK11854 358 LKEDVQAYvkdavkRAEAAPAAAAAGGGGPGLLPWPKVDFSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADI 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 290 EKIIRLRAALNAMADGRyKLSVN----DLVIKATTAALRQVPEVNAAWMGD---FIRQyKNVDISMAVATPSGLITPVIR 362
Cdd:PRK11854 438 TELEAFRKQQNAEAEKR-KLGVKitplVFIMKAVAAALEQMPRFNSSLSEDgqrLTLK-KYVNIGIAVDTPNGLVVPVFK 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 363 NTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDStseKGF 442
Cdd:PRK11854 516 DVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNG---KEF 592
|
410 420 430
....*....|....*....|....*....|....*
gi 19075255 443 KVAPIMKCTLSSDHRVVDGAMAARFTTALKKILEN 477
Cdd:PRK11854 593 APRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-483 |
2.70e-56 |
|
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: 195.86 E-value: 2.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 76 KIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKpLAVTVENEGDVAAMAdftiEDSSAKEPSAKS 155
Cdd:TIGR01348 138 KVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGD-LILTLSVAGSTPATA----PAPASAQPAAQS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 156 --GEEKSAPSSEKQSKETSSPSNVSGEERGDRV-FASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENF--KPVVAPK 230
Cdd:TIGR01348 212 paATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVdHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFvkEPSVRAQ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 231 --PSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRAALNAMADGR-Y 307
Cdd:TIGR01348 292 aaAASAAGGAPGALPWPNVDFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEgV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 308 KLSVNDLVIKATTAALRQVPEVNA--AWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARN 385
Cdd:TIGR01348 372 KLTVLHILMKAVAAALKKFPKFNAslDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 386 NKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDStseKGFKVAPIMKCTLSSDHRVVDGAMAA 465
Cdd:TIGR01348 452 GKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNG---KEFEPRLMLPLSLSYDHRVIDGADAA 528
|
410
....*....|....*...
gi 19075255 466 RFTTALKKILENPLEIML 483
Cdd:TIGR01348 529 RFTTYICESLADIRRLLL 546
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
76-483 |
1.01e-55 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 191.09 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 76 KIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAVTVENEGDVAAMADFTIEDSSAKEPSAKS 155
Cdd:PLN02528 21 KEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETLLKIMVEDSQHLRSDSLLLPTDSSNIVSLAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 156 GEEKSapssekqsketsspSNVSGeergdrVFASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENFKPVVA----PKP 231
Cdd:PLN02528 100 SDERG--------------SNLSG------VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGvvkdSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 232 SNEAAAKATTPAASAADAAAPGDYED--LPLSNMRKIIASRLAESKNMnPHYYVTVSVNMEKIIRLRAAL-NAMADGRYK 308
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQSYEDktIPLRGFQRAMVKTMTAAAKV-PHFHYVEEINVDALVELKASFqENNTDPTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 309 LSVNDLVIKATTAALRQVPEVNAAWMGDF--IRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNN 386
Cdd:PLN02528 239 HTFLPFLIKSLSMALSKYPLLNSCFNEETseIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 387 KLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVG--------TTVDTVVPDStsekgfkvapIMKCTLSSDHRV 458
Cdd:PLN02528 319 KLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGriqkvprfVDDGNVYPAS----------IMTVTIGADHRV 388
|
410 420
....*....|....*....|....*
gi 19075255 459 VDGAMAARFTTALKKILENPLEIML 483
Cdd:PLN02528 389 LDGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
189-483 |
1.13e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 181.26 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 189 SPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENFKPVVAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIA 268
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEIERIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 269 SRLAESKNMNPHYYVTVSVNMEKIIRLRAAL--NAMADGRYKLSVNDLVIKATTAALRQVPEVNAAWM--GDFIRQYKNV 344
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVlePIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTedGKTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 345 DISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILA 424
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19075255 425 VGTTVDTVVpdsTSEKGFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:PRK14843 292 VSSTIEKPV---VVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
56-476 |
5.35e-41 |
|
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: 154.79 E-value: 5.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 56 INMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKI------------------------- 110
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIrapeddtvevggvlaiigepgeags 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 111 ---------------------------------------------------------------------------LIETG 115
Cdd:TIGR02927 85 epapaapepeaapepeapapaptpaaeapapaapqaggsgeatevkmpelgesvtegtvtswlkavgdtvevdepLLEVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 116 TKDV------PV-GKPLAVTVENE------------GDVAAMADFTIEDS--------SAKEPSAKSGEEKSAPSSEKQS 168
Cdd:TIGR02927 165 TDKVdteipsPVaGTLLEIRAPEDdtvevgtvlaiiGDANAAPAEPAEEEapapseagSEPAPDPAARAPHAAPDPPAPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 169 K---ETSSPSNVSGEERGDRV-FASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDI--------ENFKPVVAPKPSNEAA 236
Cdd:TIGR02927 245 PapaKTAAPAAAAPVSSGDSGpYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVlaaakaaeEARAAAAAPAAAAAPA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 237 AKATTPAASAADAAA-PGDYEDlpLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRA-ALNAMADGR-YKLSVND 313
Cdd:TIGR02927 325 APAAAAKPAEPDTAKlRGTTQK--MNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRArAKNDFLEKNgVNLTFLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 314 LVIKATTAALRQVPEVNAAWMGDF--IRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPE 391
Cdd:TIGR02927 403 FFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 392 EYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVD--TVVPDSTSEKGFKVAPIMKCTLSSDHRVVDGAMAARFTT 469
Cdd:TIGR02927 483 ELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKrpRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLT 562
|
....*..
gi 19075255 470 ALKKILE 476
Cdd:TIGR02927 563 TIKKRLE 569
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
58-483 |
3.64e-38 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 144.90 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 58 MPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTkdvpvgkplavTVENEGDVAA 137
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-----------TVEPGTKVAI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 138 MAdfTIEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPsnvsgeergdRVFASPLARKlaeekdldlsqirgsgPNGriik 217
Cdd:PLN02226 165 IS--KSEDAASQVTPSQKIPETTDPKPSPPAEDKQKP----------KVESAPVAEK----------------PKA---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 218 vdienfkPVVAPKPSNEAAAKATTPAASAadaaapgdyEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRA 297
Cdd:PLN02226 213 -------PSSPPPPKQSAKEPQLPPKERE---------RRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 298 ALNAMADGRY--KLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTL 375
Cdd:PLN02226 277 QYKDAFYEKHgvKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 376 AKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVD--TVVPDSTSEKgfkvaPIMKCTLS 453
Cdd:PLN02226 357 INGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSrpMVVGGSVVPR-----PMMYVALT 431
|
410 420 430
....*....|....*....|....*....|
gi 19075255 454 SDHRVVDGAMAARFTTALKKILENPLEIML 483
Cdd:PLN02226 432 YDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
185-478 |
1.30e-36 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 136.85 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 185 RVFASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENFK------PVVAPKPSNEAAAKATTPAASAADAAAPGDYEDl 258
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 259 PLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRAAL--NAMADGRYKLSVNDLVIKATTAALRQVPEVNAAW--M 334
Cdd:PRK11857 80 KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVkdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 335 GDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAI 414
Cdd:PRK11857 160 TSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075255 415 INPPQACILAVGTTVDTVVpdstSEKGFKVA-PIMKCTLSSDHRVVDGAMAARFTTALKKILENP 478
Cdd:PRK11857 240 INYPELAIAGVGAIIDKAI----VKNGQIVAgKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
56-190 |
6.64e-27 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 113.09 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 56 INMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVEnEGDV 135
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLE-EGES 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19075255 136 AAmadftieDSSAKEPSAKSGEEKSAPSSEKQSKETSSPSNVSGEERGDRVFASP 190
Cdd:PRK11892 84 AS-------DAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADP 131
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
54-127 |
1.01e-24 |
|
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: 97.09 E-value: 1.01e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075255 54 TVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAV 127
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
54-127 |
1.79e-19 |
|
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: 82.42 E-value: 1.79e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075255 54 TVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAV 127
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
186-221 |
1.78e-15 |
|
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: 70.02 E-value: 1.78e-15
10 20 30
....*....|....*....|....*....|....*.
gi 19075255 186 VFASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIE 221
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
54-220 |
2.73e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 74.21 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 54 TVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTkDVPVGKPLAVtveneg 133
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAV------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 134 dvaamadftIEDSSakepsaksgeeksapssekqsketsspsnVSGEErgDRVFASPLARKLAEEkDLDLSQIRGSGPNG 213
Cdd:PRK14875 76 ---------VADAE-----------------------------VSDAE--IDAFIAPFARRFAPE-GIDEEDAGPAPRKA 114
|
....*..
gi 19075255 214 RIIKVDI 220
Cdd:PRK14875 115 RIGGRTV 121
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
54-127 |
5.78e-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: 63.77 E-value: 5.78e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075255 54 TVINMPALSPTMTTGNIGAFqKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAV 127
Cdd:pfam00364 1 TEIKSPMIGESVREGVVEWL-VKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
56-125 |
2.01e-12 |
|
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: 62.46 E-value: 2.01e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 56 INMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPL 125
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPL 70
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
322-474 |
4.99e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 52.59 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 322 ALRQVPEVNAAwmgdfirqYKNVD--------------ISMAVATPSG---LITPVIRNTHALGLAEISTLAKDYGQRAR 384
Cdd:PRK12270 183 ALKAFPNMNRH--------YAEVDgkptlvtpahvnlgLAIDLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRAR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075255 385 NNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVG----------TTVDTVvpdstSEKGfkVAPIMkcTLSS 454
Cdd:PRK12270 255 DGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGameypaefqgASEERL-----AELG--ISKVM--TLTS 325
|
170 180
....*....|....*....|..
gi 19075255 455 --DHRVVDGAMAARFttaLKKI 474
Cdd:PRK12270 326 tyDHRIIQGAESGEF---LRTI 344
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
76-127 |
3.21e-03 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 39.44 E-value: 3.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 19075255 76 KIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGtKDVPVGKPLAV 127
Cdd:PLN02983 221 KVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDG-KPVSVDTPLFV 271
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
67-127 |
3.48e-03 |
|
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: 35.85 E-value: 3.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075255 67 TGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKdVPVGKPLAV 127
Cdd:cd06850 7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVV 66
|
|
| |
