|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
51-493 |
1.79e-133 |
|
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: 393.39 E-value: 1.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 51 KVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRNVRLGTLIALMVEEGQD 130
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 131 WKQVEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRL-----------SPAARHILDTHGIDPKLA 199
Cdd:TIGR01349 81 VADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLsdkesgdrifaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 200 TPTGPRGLITKEDALNLLKTSPAAKPAPATAAPpppspaptpaapppppgsrpniPPLSIPGKPGAPGTFTEIPATNVRR 279
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATT----------------------PATYPAAAPVSTGSYEDVPLSNIRK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 280 VIAQRLTQSKTTIPHAYASVDCDMAAVMHLRKDL---AKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIH 356
Cdd:TIGR01349 219 IIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 357 ISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAV 436
Cdd:TIGR01349 299 ISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAV 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 437 GTS-RSELRLCEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:TIGR01349 379 GAVeDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
54-493 |
4.33e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 386.07 E-value: 4.33e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 54 MPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLGTLIALMVEEGqdwkq 133
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 134 vEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAARHILDTHGIDPKLATPTGPRGLITKEDA 213
Cdd:PRK11856 81 -EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 214 LNLLKTSPAAKpapataappppspaptpaapppppgsrPNIPPLSIPGKPGAPGTFTEIPATNVRRVIAQRLTQSKTTIP 293
Cdd:PRK11856 160 EAAAAAAAPAA---------------------------AAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 294 HAYASVDCDMAAVMHLRKDLAKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIHISIAVATDKGLITPIIK 373
Cdd:PRK11856 213 HFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 374 DAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGtsRSELRLCEEDQSLR 453
Cdd:PRK11856 293 DADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVG--AIVERPVVVDGEIV 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2045355337 454 TQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PRK11856 371 VRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
285-491 |
7.09e-82 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 252.85 E-value: 7.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 285 LTQSKTTIPHAYASVDCDMAAVMHLRKDL----AKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQAL--DSIHIS 358
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVykKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 359 IAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGT 438
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2045355337 439 SRSELRlcEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRM 491
Cdd:pfam00198 161 IRKRPV--VVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
51-124 |
1.96e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.49 E-value: 1.96e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045355337 51 KVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLGTLIALM 124
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
48-125 |
2.08e-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: 96.29 E-value: 2.08e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 48 SALKVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMV 125
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
51-493 |
1.79e-133 |
|
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: 393.39 E-value: 1.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 51 KVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRNVRLGTLIALMVEEGQD 130
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 131 WKQVEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRL-----------SPAARHILDTHGIDPKLA 199
Cdd:TIGR01349 81 VADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLsdkesgdrifaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 200 TPTGPRGLITKEDALNLLKTSPAAKPAPATAAPpppspaptpaapppppgsrpniPPLSIPGKPGAPGTFTEIPATNVRR 279
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATT----------------------PATYPAAAPVSTGSYEDVPLSNIRK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 280 VIAQRLTQSKTTIPHAYASVDCDMAAVMHLRKDL---AKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIH 356
Cdd:TIGR01349 219 IIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 357 ISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAV 436
Cdd:TIGR01349 299 ISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAV 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 437 GTS-RSELRLCEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:TIGR01349 379 GAVeDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
54-493 |
4.33e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 386.07 E-value: 4.33e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 54 MPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLGTLIALMVEEGqdwkq 133
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 134 vEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAARHILDTHGIDPKLATPTGPRGLITKEDA 213
Cdd:PRK11856 81 -EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 214 LNLLKTSPAAKpapataappppspaptpaapppppgsrPNIPPLSIPGKPGAPGTFTEIPATNVRRVIAQRLTQSKTTIP 293
Cdd:PRK11856 160 EAAAAAAAPAA---------------------------AAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 294 HAYASVDCDMAAVMHLRKDLAKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIHISIAVATDKGLITPIIK 373
Cdd:PRK11856 213 HFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 374 DAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGtsRSELRLCEEDQSLR 453
Cdd:PRK11856 293 DADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVG--AIVERPVVVDGEIV 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2045355337 454 TQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PRK11856 371 VRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
51-493 |
2.89e-103 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 319.11 E-value: 2.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 51 KVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRNVRLGTLIALMVEEG-- 128
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEed 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 129 ----QDWKQVEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPlRL--SPAARHILDTHGIDPKLATPT 202
Cdd:PLN02744 194 igkfKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGD-RIfaSPLARKLAEDNNVPLSSIKGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 203 GPRGLITKEDALNLLktspaakpapataappppspaptpaapppPPGSRPNIPPLSIPGKpgAPG-TFTEIPATNVRRVI 281
Cdd:PLN02744 273 GPDGRIVKADIEDYL-----------------------------ASGGKGATAPPSTDSK--APAlDYTDIPNTQIRKVT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 282 AQRLTQSKTTIPHAYASVDCDMAAVMHLRKDL-----AKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIH 356
Cdd:PLN02744 322 ASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 357 ISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNL-GMFGISGFSAVINPPQACILA 435
Cdd:PLN02744 402 INVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILA 481
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 436 VGTSRSELRLCEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PLN02744 482 VGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
285-491 |
7.09e-82 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 252.85 E-value: 7.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 285 LTQSKTTIPHAYASVDCDMAAVMHLRKDL----AKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQAL--DSIHIS 358
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVykKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 359 IAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGT 438
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2045355337 439 SRSELRlcEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRM 491
Cdd:pfam00198 161 IRKRPV--VVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
52-493 |
6.86e-71 |
|
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: 231.16 E-value: 6.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 52 VQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIAlMVEEGQDw 131
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGD-TVESGQVLA-ILEEGND- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 132 kqveipppdaaapsaaPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAARHILDTHGIDPKLATPTGPRGLITKE 211
Cdd:TIGR01347 80 ----------------ATAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 212 DALNLLKtspaakpapataappppspaptpaapppppgSRPNIPPLSIPGKPGAPGTFTE----IPATNVRRVIAQRLTQ 287
Cdd:TIGR01347 144 DIIKKTE-------------------------------APASAQPPAAAAAAAAPAAATRpeerVKMTRLRQRIAERLKE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 288 SKTTIPHAYASVDCDMAAVMHLRKDLaKEQ------IKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIHISIAV 361
Cdd:TIGR01347 193 AQNSTAMLTTFNEVDMSAVMELRKRY-KEEfekkhgVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 362 ATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGiSGFSA-VINPPQACILavGTSR 440
Cdd:TIGR01347 272 STDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFG-SLMSTpIINPPQSAIL--GMHG 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2045355337 441 SELRLCEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:TIGR01347 349 IKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
48-493 |
2.35e-66 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 219.32 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 48 SALKVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMVEE 127
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 128 GqdwkqveipppdaaapsaAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAARHILDTHGIDPKLATPTGPRGL 207
Cdd:PRK05704 80 A------------------AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 208 ITKEDALNLLKTSPaakpapataappppspaptpaapppppGSRPNIPPLSIPGKPGAPGTFTEI--PATNVRRVIAQRL 285
Cdd:PRK05704 142 VTKEDVLAALAAAA---------------------------AAPAAPAAAAPAAAPAPLGARPEErvPMTRLRKTIAERL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 286 TQSK------TTiphaYASVDcdMAAVMHLRKDLaKEQ------IKVSVNDFIIKAAAVTLKEMPEVNVTWSGDgpqalD 353
Cdd:PRK05704 195 LEAQnttamlTT----FNEVD--MTPVMDLRKQY-KDAfekkhgVKLGFMSFFVKAVVEALKRYPEVNASIDGD-----D 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 354 SI-----HISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGiSGFSA-VIN 427
Cdd:PRK05704 263 IVyhnyyDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFG-SLMSTpIIN 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045355337 428 PPQACILavGTSRSELRLCEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PRK05704 342 PPQSAIL--GMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
63-493 |
1.46e-65 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 220.85 E-value: 1.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 63 EGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMVEEGQDWKQVEIPPPDAA 142
Cdd:PRK11855 132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGD-KVSVGSLLVVIEVAAAAPAAAAAPAAAAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 143 APSAAPPAPEAVTAPAVAPIAAPTPPPPPaaatSGPLRLSPAARHILDTHGIDPKLATPTGPRGLITKEDALNLLKTSPA 222
Cdd:PRK11855 211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAP----GKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 223 AKPAPATAAPPPPSpaptpaapppppgsrpniPPLSIPGKPGA----PGTFTEIPATNVRRVIAQRLTQSKTTIPHAYAS 298
Cdd:PRK11855 287 AAAAAAAAAAAAGG------------------GGLGLLPWPKVdfskFGEIETKPLSRIKKISAANLHRSWVTIPHVTQF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 299 VDCDMAAVMHLRKDL----AKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGpQAL---DSIHISIAVATDKGLITPI 371
Cdd:PRK11855 349 DEADITDLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELtykKYFNIGFAVDTPNGLVVPV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 372 IKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGtsRSELRLCEEDQS 451
Cdd:PRK11855 428 IKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVG--KSQMKPVWDGKE 505
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2045355337 452 LRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PRK11855 506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
48-493 |
6.45e-51 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 183.28 E-value: 6.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 48 SALKVQMPALSPTmeEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLGTLIALMVEE 127
Cdd:PRK11854 205 GVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 128 GQDWKQVEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSgplrlSPAARHILDTHGIDPKLATPTGPRGL 207
Cdd:PRK11854 282 GAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHA-----TPLVRRLAREFGVNLAKVKGTGRKGR 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 208 ITKEDALNLLKTSPAAKPAPATAAPPPpspaptpaapppppGSRPNIPPLSI--PGKPGAPGtftEIPATNVRRVIAQRL 285
Cdd:PRK11854 357 ILKEDVQAYVKDAVKRAEAAPAAAAAG--------------GGGPGLLPWPKvdFSKFGEIE---EVELGRIQKISGANL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 286 TQSKTTIPHAYASVDCDMAAVMHLRKDLAKEQ------IKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGpQAL---DSIH 356
Cdd:PRK11854 420 HRNWVMIPHVTQFDKADITELEAFRKQQNAEAekrklgVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVN 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 357 ISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILav 436
Cdd:PRK11854 499 IGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAIL-- 576
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045355337 437 GTSRSELRLCEEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PRK11854 577 GVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
62-493 |
2.12e-47 |
|
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: 172.37 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 62 EEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRNVRLGTLIALMVEEGQDWKQVEIPPPDA 141
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 142 AAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAARHILDTHGIDPKLATPTGPRGLITKEDALNLLKTSP 221
Cdd:TIGR01348 208 AAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPS 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 222 AAKPAPATAAPpppspaptpaapppppGSRPNIPPLsipgkPGAP----GTFTEIPATNVRRVIAQRLTQSKTTIPHAYA 297
Cdd:TIGR01348 288 VRAQAAAASAA----------------GGAPGALPW-----PNVDfskfGEVEEVDMSRIRKISGANLTRNWTMIPHVTH 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 298 SVDCDMAAVMHLRKDLA----KEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQAL--DSIHISIAVATDKGLITPI 371
Cdd:TIGR01348 347 FDKADITEMEAFRKQQNaaveKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLIlkKYVNIGVAVDTPNGLLVPV 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 372 IKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILavGTSRSELRLCEEDQS 451
Cdd:TIGR01348 427 IKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKE 504
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2045355337 452 LRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:TIGR01348 505 FEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
52-493 |
1.08e-46 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 167.55 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 52 VQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMVEEGQdw 131
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEIDTGGA-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 132 kqveipppdaaapsaAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAArhildthgidPKLATPTGPrglitke 211
Cdd:PTZ00144 124 ---------------PPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTP----------PAAAKPPEP------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 212 dalnllktspaakpapataappppspaptpaapppppgsrPNIPPLSIPGKPGAPGTFTEIPATNVRRVIAQRLTQSKTT 291
Cdd:PTZ00144 172 ----------------------------------------APAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 292 iphaYASV----DCDMAAVMHLRKDLAKE-QIKVSVN----DFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIHISIAVA 362
Cdd:PTZ00144 212 ----CAMLttfnECDMSALMELRKEYKDDfQKKHGVKlgfmSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 363 TDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGiSGFSA-VINPPQACILAVGTSRS 441
Cdd:PTZ00144 288 TPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFG-SLMGTpIINPPQSAILGMHAIKK 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2045355337 442 ELRLCEEDQSLRtqQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PTZ00144 367 RPVVVGNEIVIR--PIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
63-494 |
5.62e-42 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 154.49 E-value: 5.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 63 EGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLG-TLIALMVEEGQDwkqveipppda 141
Cdd:PLN02528 12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQH----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 142 aapsaaPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRlSPAARHILDTHGIDPKLATPTGPRGLITKEDALNLLKTSP 221
Cdd:PLN02528 80 ------LRSDSLLLPTDSSNIVSLAESDERGSNLSGVLS-TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 222 AAKPAPATAAPPPPSPAPTPAAPPPPPGSRPNipplsipgkpgapgtFTEIPATNVRRVIAQRLTQSkTTIPHAYAS--V 299
Cdd:PLN02528 153 VVKDSSSAEEATIAEQEEFSTSVSTPTEQSYE---------------DKTIPLRGFQRAMVKTMTAA-AKVPHFHYVeeI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 300 DCDmaAVMHLRKDLAKEQ----IKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQA--LDSIHISIAVATDKGLITPIIK 373
Cdd:PLN02528 217 NVD--ALVELKASFQENNtdptVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIrlKGSHNIGVAMATEHGLVVPNIK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 374 DAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGTSRSELRLCEEDQSLR 453
Cdd:PLN02528 295 NVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYP 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2045355337 454 TqQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMALA 494
Cdd:PLN02528 375 A-SIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLH 414
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
179-491 |
1.02e-41 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 152.37 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 179 LRLSPAARHILDTHGIDPKLATPTGPRGLITKEDALNLLKTSPAAKPAPATAAPPPPSPaptpaapppppgsrpnippls 258
Cdd:PRK14843 49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEE--------------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 259 IPGKPGAPGTFTEIPATNVRRVIAQRLTQSKTTIPHAYASVDCDMAAVMHLRKD-----LAKEQIKVSVNDFIIKAAAVT 333
Cdd:PRK14843 108 VPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvlepiMEATGKKTTVTDLLSLAVVKT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 334 LKEMPEVNVTWSGDGPQAL--DSIHISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSI 411
Cdd:PRK14843 188 LMKHPYINASLTEDGKTIIthNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 412 SNLGMFGISGFSAVINPPQACILAVGTSRSELRLCEEDQSLRTqqLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRM 491
Cdd:PRK14843 268 SNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRP--IMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISM 345
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
46-486 |
1.31e-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: 156.71 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 46 GVSALKVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEgSRNVRLGTLIALM- 124
Cdd:TIGR02927 123 SGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIg 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 125 ----------VEEGQDWKQVEIPPPDAAAPSAAPPAPEAVTAPAVAPIAAPTPPPPPAAATSGPLRLSPAARHILDTHGI 194
Cdd:TIGR02927 202 danaapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 195 DPKLATPTGPRGLITKEDALnllktspaakpapataAPPPPSPAPTPAAPPPPPGSRPNIPPLSipGKPGAPGTF----T 270
Cdd:TIGR02927 282 DLSTVKGTGVGGRIRKQDVL----------------AAAKAAEEARAAAAAPAAAAAPAAPAAA--AKPAEPDTAklrgT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 271 EIPATNVRRVIAQRLTQSKTTIPHAYASVDCDMAAVMHLRKD-----LAKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWS 345
Cdd:TIGR02927 344 TQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYN 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 346 GDGPQAL--DSIHISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFS 423
Cdd:TIGR02927 424 AETKEVTyhDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDT 503
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045355337 424 AVINPPQACILAVGTSRSELR-LCEED--QSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLE 486
Cdd:TIGR02927 504 PILNPPQAAILGTGAIVKRPRvIKDEDggESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
54-493 |
6.60e-36 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 138.73 E-value: 6.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 54 MPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMVEEGQDWKQ 133
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-TVEPGTKVAIISKSEDAASQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 134 VeipppdaaapsaappapeavtapavapiaaptpppppaaatsGPLRLSPAArhildthgIDPKLATPTGPRGLITKEDA 213
Cdd:PLN02226 175 V------------------------------------------TPSQKIPET--------TDPKPSPPAEDKQKPKVESA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 214 lnllktspaakpapataappppspaptpAAPPPPPGSRPNIPPLSIPGKPGAPGTFTE--IPATNVRRVIAQRLTQSKTT 291
Cdd:PLN02226 205 ----------------------------PVAEKPKAPSSPPPPKQSAKEPQLPPKERErrVPMTRLRKRVATRLKDSQNT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 292 IPHAYASVDCDMAAVMHLR---KD--LAKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSGDGPQALDSIHISIAVATDKG 366
Cdd:PLN02226 257 FALLTTFNEVDMTNLMKLRsqyKDafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 367 LITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVGTSRSelRLC 446
Cdd:PLN02226 337 LVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVS--RPM 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2045355337 447 EEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQRMAL 493
Cdd:PLN02226 415 VVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
182-489 |
7.15e-32 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 124.14 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 182 SPAARHILDTHGIDPKLATPTGPRGLITKEDALNLLKTSPAAKPAPATAAPPPPSPaptpaapppppgSRPNIPPLSIPG 261
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQ------------AAKTAAPAAAPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 262 KPGAPGTfteiPATNVRRVIAQRLTQSKTTIphAYASV--DCDMAAVMHLRKD-----LAKEQIKVSVNDFIIKAAAVTL 334
Cdd:PRK11857 73 KLEGKRE----KVAPIRKAIARAMTNSWSNV--AYVNLvnEIDMTKLWDLRKSvkdpvLKTEGVKLTFLPFIAKAILIAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 335 KEMPEVNVTWSgDGPQAL---DSIHISIAVATDKGLITPIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSI 411
Cdd:PRK11857 147 KEFPIFAAKYD-EATSELvypDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTI 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 412 SNLGMFGISGFSAVINPPQACILAVGTSRSELRLceEDQSLRTQQLMRVTLSSDGRLVDDELASRFLDKFRENLEKPQ 489
Cdd:PRK11857 226 TNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIV--KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPE 301
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
49-130 |
1.74e-31 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 126.19 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 49 ALKVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRNVRLGTLIALMVEEG 128
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEG 81
|
..
gi 2045355337 129 QD 130
Cdd:PRK11892 82 ES 83
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
51-124 |
1.96e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.49 E-value: 1.96e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045355337 51 KVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLGTLIALM 124
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
48-125 |
2.08e-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: 96.29 E-value: 2.08e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 48 SALKVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMV 125
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
52-124 |
6.43e-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: 72.25 E-value: 6.43e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045355337 52 VQMPALSPTMEEGnIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALM 124
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGD-TVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
48-128 |
6.20e-15 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 76.14 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 48 SALKVQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIALMVEE 127
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADA 79
|
.
gi 2045355337 128 G 128
Cdd:PRK14875 80 E 80
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
52-113 |
4.04e-14 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 67.08 E-value: 4.04e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045355337 52 VQMPALSPTMEEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSR 113
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
64-122 |
1.85e-08 |
|
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: 50.88 E-value: 1.85e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2045355337 64 GNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrNVRLGTLIA 122
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD-QVEAGQLLV 65
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
180-214 |
1.22e-07 |
|
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: 47.68 E-value: 1.22e-07
10 20 30
....*....|....*....|....*....|....*
gi 2045355337 180 RLSPAARHILDTHGIDPKLATPTGPRGLITKEDAL 214
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
244-437 |
6.84e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 52.20 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 244 PPPPPGSRPNIPPLSIPGKPGAPGTFTEIPATNVRRVIAQRLTQSKTTIPHAYASVDCDM----------------AAVM 307
Cdd:PRK12270 72 PAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMdaslevptatsvravpAKLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 308 ---------HLRKdlaKEQIKVSVNDFIIKAAAVTLKEMPEVNVTWSG-DG-PQALDSIHISIAVATD-------KGLIT 369
Cdd:PRK12270 152 idnrivinnHLKR---TRGGKVSFTHLIGYALVQALKAFPNMNRHYAEvDGkPTLVTPAHVNLGLAIDlpkkdgsRQLVV 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045355337 370 PIIKDAANKGVQEISASAKALAQKARDGKLLPEEYQGGSFSISNLGMFGISGFSAVINPPQACILAVG 437
Cdd:PRK12270 229 PAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
49-128 |
2.21e-06 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 50.39 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045355337 49 ALKVQMPALSPTmeEGNIVKWLKREGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSRnVRLGTLIALMVEEG 128
Cdd:PRK11854 2 AIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDK-VETGALIMIFESAD 78
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
73-129 |
4.75e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 37.57 E-value: 4.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045355337 73 EGEAVAAGDALCEIETDKAVVTMESNDDGVLAKILMEEGSrnvrlgtlialMVEEGQ 129
Cdd:COG0511 85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ-----------PVEYGQ 130
|
|
| |
