|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
39-463 |
4.99e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 397.62 E-value: 4.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 39 IREIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAETED 118
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 119 EIADAKAKasggggggdskappaspptaaVEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKV 198
Cdd:PRK11856 82 AEAAAAAE---------------------AAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 199 ELAGLVGSGPMGRIVAKDVEAVAAGGGVQAAVAVKEVVAAPGV--ELGSVVPFTTMQGAVSRNMVES-LGVPTFRVGYTI 275
Cdd:PRK11856 141 DLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAaaEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 276 STDALDALYKKIKS--KGVTMTALLAKATALALAKHPVVNSSCrDGNSFVYNSSINVAVAVAIDGGLITPVLQNADKVDI 353
Cdd:PRK11856 221 DVTALLALRKQLKAigVKLTVTDFLIKAVALALKKFPELNASW-DDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 354 YSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVAtKDGRIGMKNQMQVN 433
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLS 378
|
410 420 430
....*....|....*....|....*....|
gi 1032298090 434 VTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PRK11856 379 LSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
41-460 |
5.81e-86 |
|
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: 270.13 E-value: 5.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEG--GVaPVGSAIALLAETED 118
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtkDV-PVNKPIAVLVEEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 119 EIADAKAKASGGGGGGDSKAPPASPPTaaveAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKV 198
Cdd:TIGR01349 80 DVADAFKNYKLESSASPAPKPSEIAPT----APPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 199 ELAGLVGSGPMGRIVAKDVE-----AVAAGGGVQAAVAVKEVVAAPGVELGSV--VPFTTMQGAVSRNMVES-LGVPTFR 270
Cdd:TIGR01349 156 DLSAVAGSGPNGRIVKKDIEsfvpqSPASANQQAAATTPATYPAAAPVSTGSYedVPLSNIRKIIAKRLLESkQTIPHYY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 271 VGYTISTDALDALYKKI------KSKgVTMTALLAKATALALAKHPVVNSSCRDgNSFVYNSSINVAVAVAIDGGLITPV 344
Cdd:TIGR01349 236 VSIECNVDKLLALRKELnamaseVYK-LSVNDFIIKASALALREVPEANSSWTD-NFIRRYKNVDISVAVATPDGLITPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 345 LQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVATKDGRI 424
Cdd:TIGR01349 314 VRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEK 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 1032298090 425 GMK--NQMQVNVTADHRVIYGADLAQFLQTLASIIEDP 460
Cdd:TIGR01349 394 GFAvaSIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENP 431
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
260-463 |
6.23e-56 |
|
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: 184.67 E-value: 6.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 260 MVESL-GVPTFRVGYTISTDALDALYKKIKSKG------VTMTALLAKATALALAKHPVVNSSC-RDGNSFVYNSSINVA 331
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAadeetkLTFLPFLVKAVALALKKFPELNASWdGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 332 VAVAIDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGA 411
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032298090 412 SQPSVVAtKDGRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
41-113 |
3.54e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 98.25 E-value: 3.54e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALL 113
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
39-114 |
6.31e-24 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 94.75 E-value: 6.31e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032298090 39 IREIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLA 114
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
39-463 |
4.99e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 397.62 E-value: 4.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 39 IREIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAETED 118
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 119 EIADAKAKasggggggdskappaspptaaVEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKV 198
Cdd:PRK11856 82 AEAAAAAE---------------------AAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 199 ELAGLVGSGPMGRIVAKDVEAVAAGGGVQAAVAVKEVVAAPGV--ELGSVVPFTTMQGAVSRNMVES-LGVPTFRVGYTI 275
Cdd:PRK11856 141 DLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAaaEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 276 STDALDALYKKIKS--KGVTMTALLAKATALALAKHPVVNSSCrDGNSFVYNSSINVAVAVAIDGGLITPVLQNADKVDI 353
Cdd:PRK11856 221 DVTALLALRKQLKAigVKLTVTDFLIKAVALALKKFPELNASW-DDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 354 YSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVAtKDGRIGMKNQMQVN 433
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLS 378
|
410 420 430
....*....|....*....|....*....|
gi 1032298090 434 VTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PRK11856 379 LSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
41-460 |
5.81e-86 |
|
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: 270.13 E-value: 5.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEG--GVaPVGSAIALLAETED 118
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtkDV-PVNKPIAVLVEEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 119 EIADAKAKASGGGGGGDSKAPPASPPTaaveAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKV 198
Cdd:TIGR01349 80 DVADAFKNYKLESSASPAPKPSEIAPT----APPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 199 ELAGLVGSGPMGRIVAKDVE-----AVAAGGGVQAAVAVKEVVAAPGVELGSV--VPFTTMQGAVSRNMVES-LGVPTFR 270
Cdd:TIGR01349 156 DLSAVAGSGPNGRIVKKDIEsfvpqSPASANQQAAATTPATYPAAAPVSTGSYedVPLSNIRKIIAKRLLESkQTIPHYY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 271 VGYTISTDALDALYKKI------KSKgVTMTALLAKATALALAKHPVVNSSCRDgNSFVYNSSINVAVAVAIDGGLITPV 344
Cdd:TIGR01349 236 VSIECNVDKLLALRKELnamaseVYK-LSVNDFIIKASALALREVPEANSSWTD-NFIRRYKNVDISVAVATPDGLITPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 345 LQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVATKDGRI 424
Cdd:TIGR01349 314 VRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEK 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 1032298090 425 GMK--NQMQVNVTADHRVIYGADLAQFLQTLASIIEDP 460
Cdd:TIGR01349 394 GFAvaSIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENP 431
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
40-463 |
1.73e-68 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 227.81 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 40 REIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVA-PVGSAIALLAETED 118
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEiKVGEVIAITVEEEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 119 EIADAKAKASGGGGGGDSKAPPaspptaavEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKV 198
Cdd:PLN02744 193 DIGKFKDYKPSSSAAPAAPKAK--------PSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 199 ELAGLVGSGPMGRIVAKDVEAVAAGGGVQAAVAVKEVVAAPGveLGSV-VPFTTMQGAVSRNMVES-LGVPTFRVGYTIS 276
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPA--LDYTdIPNTQIRKVTASRLLQSkQTIPHYYLTVDTR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 277 TDA-------LDALYKKIKSKGVTMTALLAKATALALAKHPVVNSSCRDGNSFVYNsSINVAVAVAIDGGLITPVLQNAD 349
Cdd:PLN02744 343 VDKlmalrsqLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH-NVNINVAVQTENGLYVPVVKDAD 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 350 KVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNL-GMFGVDRFDAILPPGTGAIMAVGASQPSVV-ATKDGRIGMK 427
Cdd:PLN02744 422 KKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIpGSGPDQYNFA 501
|
410 420 430
....*....|....*....|....*....|....*.
gi 1032298090 428 NQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESM 537
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
260-463 |
6.23e-56 |
|
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: 184.67 E-value: 6.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 260 MVESL-GVPTFRVGYTISTDALDALYKKIKSKG------VTMTALLAKATALALAKHPVVNSSC-RDGNSFVYNSSINVA 331
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAadeetkLTFLPFLVKAVALALKKFPELNASWdGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 332 VAVAIDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGA 411
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1032298090 412 SQPSVVAtKDGRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
52-463 |
4.72e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 183.87 E-value: 4.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 52 TEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLaETEDEIAdakakasggg 131
Cdd:PRK11855 131 TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI-EVAAAAP---------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 132 gggdskapPASPPTAAVEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKVELAGLVGSGPMGR 211
Cdd:PRK11855 200 --------AAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 212 IVAKDVEAVAAGGGVQAAVAVKEVVAAPGVELGS---------------VVPFTTMQGAVSRNMVESLgVPTFRVGYTIS 276
Cdd:PRK11855 272 ITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLlpwpkvdfskfgeieTKPLSRIKKISAANLHRSW-VTIPHVTQFDE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 277 TD--ALDALYKKIK----SKGV--TMTALLAKATALALAKHPVVNSSC-RDGNSFVYNSSINVAVAVAIDGGLITPVLQN 347
Cdd:PRK11855 351 ADitDLEALRKQLKkeaeKAGVklTMLPFFIKAVVAALKEFPVFNASLdEDGDELTYKKYFNIGFAVDTPNGLVVPVIKD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 348 ADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQpsvvaTK----DGR 423
Cdd:PRK11855 431 VDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQ-----MKpvwdGKE 505
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1032298090 424 IGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PRK11855 506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRM 545
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
41-465 |
1.22e-44 |
|
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: 161.05 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAETEDei 120
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 121 adakakasggggggdskappaspptaaVEAPVSVEKKVAAAPVSIKAVAASAvhpaSEGGKRIVASPYAKKLAKELKVEL 200
Cdd:TIGR01347 80 ---------------------------ATAAPPAKSGEEKEETPAASAAAAP----TAAANRPSLSPAARRLAKEHGIDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 201 AGLVGSGPMGRIVAKDVEAVAAGGGVQAAVAVKEVVAAPGVELGSV--VPFTTMQGAVSRNMVESLG----VPTFRVGYT 274
Cdd:TIGR01347 129 SAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAATRPEerVKMTRLRQRIAERLKEAQNstamLTTFNEVDM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 275 ISTDALDALYKK--IKSKGVTM--TALLAKATALALAKHPVVNSSCrDGNSFVYNSSINVAVAVAIDGGLITPVLQNADK 350
Cdd:TIGR01347 209 SAVMELRKRYKEefEKKHGVKLgfMSFFVKAVVAALKRFPEVNAEI-DGDDIVYKDYYDISVAVSTDRGLVVPVVRNADR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 351 VDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVATkDGRIGMKNQM 430
Cdd:TIGR01347 288 MSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAV-NGQIEIRPMM 366
|
410 420 430
....*....|....*....|....*....|....*
gi 1032298090 431 QVNVTADHRVIYGADLAQFLQTLASIIEDPKDLTF 465
Cdd:TIGR01347 367 YLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
37-463 |
3.48e-42 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 158.24 E-value: 3.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 37 AKIREIFMPALSSTmtEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLaet 116
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF--- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 117 EDEIAdakakasggggggdskAPPASPPTAAVEAPVSVEKKvAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKEL 196
Cdd:PRK11854 279 EVEGA----------------APAAAPAKQEAAAPAPAAAK-AEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREF 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 197 KVELAGLVGSGPMGRIVAKDVEAvAAGGGVQAAVAVKEVVAAPGVELG---------------SVVPFTTMQGAVSRNMV 261
Cdd:PRK11854 342 GVNLAKVKGTGRKGRILKEDVQA-YVKDAVKRAEAAPAAAAAGGGGPGllpwpkvdfskfgeiEEVELGRIQKISGANLH 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 262 ESLgVPTFRVGYTISTD--ALDALYKK------IKSKGV--TMTALLAKATALALAKHPVVNSS-CRDGNSFVYNSSINV 330
Cdd:PRK11854 421 RNW-VMIPHVTQFDKADitELEAFRKQqnaeaeKRKLGVkiTPLVFIMKAVAAALEQMPRFNSSlSEDGQRLTLKKYVNI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 331 AVAVAIDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVG 410
Cdd:PRK11854 500 GIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVS 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1032298090 411 ASQPSVVATKDgRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PRK11854 580 KSAMEPVWNGK-EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
181-460 |
9.54e-42 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 151.60 E-value: 9.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 181 KRIVASPYAKKLAKELKVELAGLVGSGPMGRIVAKDVEAV---------AAGGGVQAAVAVKEVVAAPGVELgSVVPFTT 251
Cdd:PRK14843 47 NVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALlpeniendsIKSPAQIEKVEEVPDNVTPYGEI-ERIPMTP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 252 MQGAVSRNMVES-LGVPTFRVGYTISTDALDALYKKI-------KSKGVTMTALLAKATALALAKHPVVNSS-CRDGNSF 322
Cdd:PRK14843 126 MRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKVlepimeaTGKKTTVTDLLSLAVVKTLMKHPYINASlTEDGKTI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 323 VYNSSINVAVAVAIDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPG 402
Cdd:PRK14843 206 ITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQP 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 403 TGAIMAVGAS--QPSVVatkDGRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDP 460
Cdd:PRK14843 286 NSAILGVSSTieKPVVV---NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
37-463 |
1.17e-34 |
|
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: 136.16 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 37 AKIREIFMPALSStMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAET 116
Cdd:TIGR01348 114 SGVQEVTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 117 EdeiadakakasggggGGDSKAPPASPPTAAVEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIV-ASPYAKKLAKE 195
Cdd:TIGR01348 193 G---------------STPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDhAAPAVRRLARE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 196 LKVELAGLVGSGPMGRIVAKDVEAV-------AAGGGVQAAVAVKEVVAAPGVEL---GSV--VPFTTMQGAVSRNMVES 263
Cdd:TIGR01348 258 FGVDLSAVKGTGIKGRILREDVQRFvkepsvrAQAAAASAAGGAPGALPWPNVDFskfGEVeeVDMSRIRKISGANLTRN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 264 -LGVPtfRVGYTISTD--ALDALYKKIKSKG------VTMTALLAKATALALAKHPVVNSSCR-DGNSFVYNSSINVAVA 333
Cdd:TIGR01348 338 wTMIP--HVTHFDKADitEMEAFRKQQNAAVekegvkLTVLHILMKAVAAALKKFPKFNASLDlGGEQLILKKYVNIGVA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 334 VAIDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQ 413
Cdd:TIGR01348 416 VDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSG 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1032298090 414 PSVVATKDgRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:TIGR01348 496 MEPVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
53-465 |
1.21e-32 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 128.30 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 53 EGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIaLLAETEDEiadakakasgggg 132
Cdd:PLN02528 12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETL-LKIMVEDS------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 133 ggdskappaspptaavEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGkrIVASPYAKKLAKELKVELAGLVGSGPMGRI 212
Cdd:PLN02528 78 ----------------QHLRSDSLLLPTDSSNIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 213 VAKDVEAVAAGGGVQAAVAVKEVVAAPGVELGS--------------VVPFTTMQGAVSRNMVESLGVPTFRVGYTISTD 278
Cdd:PLN02528 140 LKEDVLKYAAQKGVVKDSSSAEEATIAEQEEFStsvstpteqsyedkTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 279 ALDALYKKIKSKG------VTMTALLAKATALALAKHPVVNSsCRDGNSF--VYNSSINVAVAVAIDGGLITPVLQNADK 350
Cdd:PLN02528 220 ALVELKASFQENNtdptvkHTFLPFLIKSLSMALSKYPLLNS-CFNEETSeiRLKGSHNIGVAMATEHGLVVPNIKNVQS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 351 VDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVATKDGRIGMKNQM 430
Cdd:PLN02528 299 LSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIM 378
|
410 420 430
....*....|....*....|....*....|....*
gi 1032298090 431 QVNVTADHRVIYGADLAQFLQTLASIIEDPKDLTF 465
Cdd:PLN02528 379 TVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
41-463 |
1.50e-32 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 127.64 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAEtedei 120
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 121 adakakasggggggdskappaspptaavEAPVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKVEL 200
Cdd:PRK05704 79 ----------------------------GAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 201 AGLVGSGPMGRIVAKDVEAVAAGGGVQAAVAVKEVVAAPGVELGSV----VPFTTMQGAVSRNMVESLG----VPTFRvg 272
Cdd:PRK05704 131 SAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARpeerVPMTRLRKTIAERLLEAQNttamLTTFN-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 273 yTISTDALDALYKKIK-----------------SKGVTmtallakataLALAKHPVVNSSCrDGNSFVYNSSINVAVAVA 335
Cdd:PRK05704 209 -EVDMTPVMDLRKQYKdafekkhgvklgfmsffVKAVV----------EALKRYPEVNASI-DGDDIVYHNYYDIGIAVG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 336 IDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPS 415
Cdd:PRK05704 277 TPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKER 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1032298090 416 VVAtKDGRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PRK05704 357 PVA-VNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
42-461 |
5.48e-28 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 115.16 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 42 IFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAETEDEIA 121
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 122 DAKAKASGGGgggdskappaspptaavEAPVSVEKKVAAAPVSIKAVAASAVHPASEggKRIVASPYAKKLAKELKVELA 201
Cdd:PTZ00144 127 AAPAAAAAAK-----------------AEKTTPEKPKAAAPTPEPPAASKPTPPAAA--KPPEPAPAAKPPPTPVARADP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 202 GlVGSGPMGRIVAKDVEAVAAgggvqaavavkevvaapgvelgsvvpfttmqgavSRNMVESLgvPTFRvgyTISTDALD 281
Cdd:PTZ00144 188 R-ETRVPMSRMRQRIAERLKA----------------------------------SQNTCAML--TTFN---ECDMSALM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 282 AL---YKKIKSK--GVT--MTALLAKATALALAKHPVVNSSCrDGNSFVYNSSINVAVAVAIDGGLITPVLQNADKVDIY 354
Cdd:PTZ00144 228 ELrkeYKDDFQKkhGVKlgFMSAFVKASTIALKKMPIVNAYI-DGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 355 SLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGASQPSVVAtKDGRIGMKNQMQVNV 434
Cdd:PTZ00144 307 EIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVV-VGNEIVIRPIMYLAL 385
|
410 420
....*....|....*....|....*..
gi 1032298090 435 TADHRVIYGADLAQFLQTLASIIEDPK 461
Cdd:PTZ00144 386 TYDHRLIDGRDAVTFLKKIKDLIEDPA 412
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
41-113 |
3.54e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 98.25 E-value: 3.54e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALL 113
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
39-114 |
6.31e-24 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 94.75 E-value: 6.31e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032298090 39 IREIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLA 114
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
41-463 |
1.59e-23 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 102.91 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAETEDEI 120
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 121 ADAKAKASGGGGGGDSKAPPASPPTA-AVE-APVSVEKKVAAAPVSIKAVAASAVHPASEGGKRIVASPYAKKLAKELKv 198
Cdd:PLN02226 173 SQVTPSQKIPETTDPKPSPPAEDKQKpKVEsAPVAEKPKAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLK- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 199 elaglvgsgpmgrivakDVEavaagggvqaavavkevvaapgvelgsvvpfTTMQGAVSRNMVESLGVPTFRVGYTistd 278
Cdd:PLN02226 252 -----------------DSQ-------------------------------NTFALLTTFNEVDMTNLMKLRSQYK---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 279 alDALYKKIKSKgVTMTALLAKATALALAKHPVVNSSCrDGNSFVYNSSINVAVAVAIDGGLITPVLQNADKVDIYSLSR 358
Cdd:PLN02226 280 --DAFYEKHGVK-LGLMSGFIKAAVSALQHQPVVNAVI-DGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 359 KWKELVDKARAKQLQPQEYNTGTFTLSNLGMFGVDRFDAILPPGTGAIMAVGA--SQPSVVAtkdGRIGMKNQMQVNVTA 436
Cdd:PLN02226 356 TINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSivSRPMVVG---GSVVPRPMMYVALTY 432
|
410 420
....*....|....*....|....*..
gi 1032298090 437 DHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PLN02226 433 DHRLIDGREAVYFLRRVKDVVEDPQRL 459
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
182-463 |
6.75e-23 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 98.71 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 182 RIVASPYAKKLAKELKVELAGLVGSGPMGRIVAKDVE------------AVAAGGGVQAAVAVKEVVAAPGVEL-GSVVP 248
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVEnfikslksaptpAEAASVSSAQQAAKTAAPAAAPPKLeGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 249 FTTMQGAVSRNMVESLGvptfRVGYT-----ISTDALDALYKKI-----KSKGV--TMTALLAKATALALAKHPVVNSSC 316
Cdd:PRK11857 81 VAPIRKAIARAMTNSWS----NVAYVnlvneIDMTKLWDLRKSVkdpvlKTEGVklTFLPFIAKAILIALKEFPIFAAKY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 317 RDGNS-FVYNSSINVAVAVAIDGGLITPVLQNADKVDIYSLSRKWKELVDKARAKQLQPQEYNTGTFTLSNLG----MFG 391
Cdd:PRK11857 157 DEATSeLVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGsvgsLYG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032298090 392 VdrfDAILPPGTgAIMAVGASQPSVVaTKDGRIGMKNQMQVNVTADHRVIYGADLAQFLQTLASIIEDPKDL 463
Cdd:PRK11857 237 V---PVINYPEL-AIAGVGAIIDKAI-VKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
41-176 |
2.09e-18 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 87.28 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEG--GVApVGSAIALLAEtED 118
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGteGVK-VNTPIAVLLE-EG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032298090 119 EiaDAKAKASGGGGGGDSKAPPASPPTAAVEAPVSVEKKVAAAPVSikAVAASAVHPA 176
Cdd:PRK11892 82 E--SASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAA--EVAADPDIPA 135
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
39-117 |
1.19e-15 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 78.06 E-value: 1.19e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032298090 39 IREIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALLAETE 117
Cdd:PRK14875 2 ITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
183-218 |
2.61e-11 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 58.08 E-value: 2.61e-11
10 20 30
....*....|....*....|....*....|....*.
gi 1032298090 183 IVASPYAKKLAKELKVELAGLVGSGPMGRIVAKDVE 218
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
41-107 |
3.04e-11 |
|
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: 58.99 E-value: 3.04e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032298090 41 EIFMPALSSTMTEGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVG 107
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
41-113 |
4.68e-11 |
|
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: 58.38 E-value: 4.68e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032298090 41 EIFMPALSSTMTEGkIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALL 113
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
246-453 |
6.01e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 61.83 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 246 VVPFTTMQGAVSRNMVESLGVPT---FRvgyTISTDALD--------------------------ALYKKIKSkgvtmta 296
Cdd:PRK12270 117 VTPLRGAAAAVAKNMDASLEVPTatsVR---AVPAKLLIdnrivinnhlkrtrggkvsfthligyALVQALKA------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 297 llakatalalakHPVVNSSCR--DGN-SFVYNSSINVAVAVAI---DGG--LITPVLQNADKVDIYSLSRKWKELVDKAR 368
Cdd:PRK12270 187 ------------FPNMNRHYAevDGKpTLVTPAHVNLGLAIDLpkkDGSrqLVVPAIKGAETMDFAQFWAAYEDIVRRAR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032298090 369 AKQLQPQEYNTGTFTLSNLGMFG----VDRfdaiLPPGTGAIMAVGA---------SQPSVVAtkdgRIGMKNQMQVNVT 435
Cdd:PRK12270 255 DGKLTADDFQGTTISLTNPGGIGtvhsVPR----LMKGQGAIIGVGAmeypaefqgASEERLA----ELGISKVMTLTST 326
|
250
....*....|....*...
gi 1032298090 436 ADHRVIYGADLAQFLQTL 453
Cdd:PRK12270 327 YDHRIIQGAESGEFLRTI 344
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
46-113 |
1.37e-04 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 40.09 E-value: 1.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032298090 46 ALSSTMTeGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEGGVAPVGSAIALL 113
Cdd:cd06850 1 EVTAPMP-GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
46-101 |
8.05e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 41.75 E-value: 8.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1032298090 46 ALSSTMTeGKIVSWVKSEGDKLNKGESVVVVESDKADMDVETFYDGYLAAIMVEEG 101
Cdd:PRK09282 524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
|
|
| |
