|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
83-512 |
1.20e-171 |
|
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: 491.23 E-value: 1.20e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKDVPVGQLLCIIVPDQGSV 162
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 163 A-AFANFKDDgaaaaPAAPAAAPAPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQLR 241
Cdd:TIGR01349 82 AdAFKNYKLE-----SSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 242 LQG-KGSGVHGSIKSGDL---------AGQKAAAKPAAAAPAKAPRAAGARYEDIPVTNMRAVIAKRLLESKTQLPHYYV 311
Cdd:TIGR01349 157 LSAvAGSGPNGRIVKKDIesfvpqspaSANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 312 TVQCQVDKLLKFRAKVNKKYEKQgARVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVF 391
Cdd:TIGR01349 237 SIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 392 NADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPDSLKGF 471
Cdd:TIGR01349 316 NADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGF 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 20129315 472 KEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:TIGR01349 396 AVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-512 |
7.66e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 413.87 E-value: 7.66e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 6 ATTRNELGALRSVLLRSNNATYVRRSTGNVVVRALSSQLINSRKLQ----SIRSKLNTSQSP--VTWSYNFARAyANLPE 79
Cdd:PLN02744 33 NSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLGLFGSNISRTARKngspMTGSGLFKSLSSsqMQSARGFSSS-SDLPP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 80 HIRVPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKDVPVGQLLCIIVPDQ 159
Cdd:PLN02744 112 HQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 160 GSVAAFANFKDDGaaaapaapAAAPAPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQ 239
Cdd:PLN02744 192 EDIGKFKDYKPSS--------SAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 240 LRLQG-KGSGVHGSIKSGDLAG-QKAAAKPAAAAPAKAPRAAGARYEDIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQV 317
Cdd:PLN02744 264 VPLSSiKGTGPDGRIVKADIEDyLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 318 DKLLKFRAKVNKKYEKQGA-RVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVFNADRK 396
Cdd:PLN02744 344 DKLMALRSQLNSLQEASGGkKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 397 GVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNL-GMFGVNQFAAVINPPQSCILAIGTTTKQLVadPDSLKG-FKEV 474
Cdd:PLN02744 424 GLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVI--PGSGPDqYNFA 501
|
490 500 510
....*....|....*....|....*....|....*...
gi 20129315 475 NMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
299-510 |
3.36e-91 |
|
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: 277.12 E-value: 3.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 299 LLESKTQLPHYYVTVQCQVDKLLKFRAKVNKKYEKQGARVSVNDFIIKAVAIASLKVPEANSAWMDT--VIRKYDDVDVS 376
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 377 VAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGT 456
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 20129315 457 TTKQLVADPDslkGFKEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNM 510
Cdd:pfam00198 161 IRKRPVVVDG---EIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
83-155 |
7.47e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 105.95 E-value: 7.47e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCII 155
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
83-156 |
2.13e-23 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 93.59 E-value: 2.13e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCIIV 156
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
83-512 |
1.20e-171 |
|
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: 491.23 E-value: 1.20e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKDVPVGQLLCIIVPDQGSV 162
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 163 A-AFANFKDDgaaaaPAAPAAAPAPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQLR 241
Cdd:TIGR01349 82 AdAFKNYKLE-----SSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 242 LQG-KGSGVHGSIKSGDL---------AGQKAAAKPAAAAPAKAPRAAGARYEDIPVTNMRAVIAKRLLESKTQLPHYYV 311
Cdd:TIGR01349 157 LSAvAGSGPNGRIVKKDIesfvpqspaSANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 312 TVQCQVDKLLKFRAKVNKKYEKQgARVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVF 391
Cdd:TIGR01349 237 SIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 392 NADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPDSLKGF 471
Cdd:TIGR01349 316 NADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGF 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 20129315 472 KEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:TIGR01349 396 AVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-512 |
7.66e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 413.87 E-value: 7.66e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 6 ATTRNELGALRSVLLRSNNATYVRRSTGNVVVRALSSQLINSRKLQ----SIRSKLNTSQSP--VTWSYNFARAyANLPE 79
Cdd:PLN02744 33 NSTRSSLGKGDDIAKRRGYPPLERRSQPKVSSLGLFGSNISRTARKngspMTGSGLFKSLSSsqMQSARGFSSS-SDLPP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 80 HIRVPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKDVPVGQLLCIIVPDQ 159
Cdd:PLN02744 112 HQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 160 GSVAAFANFKDDGaaaapaapAAAPAPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQ 239
Cdd:PLN02744 192 EDIGKFKDYKPSS--------SAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 240 LRLQG-KGSGVHGSIKSGDLAG-QKAAAKPAAAAPAKAPRAAGARYEDIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQV 317
Cdd:PLN02744 264 VPLSSiKGTGPDGRIVKADIEDyLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 318 DKLLKFRAKVNKKYEKQGA-RVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVFNADRK 396
Cdd:PLN02744 344 DKLMALRSQLNSLQEASGGkKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 397 GVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNL-GMFGVNQFAAVINPPQSCILAIGTTTKQLVadPDSLKG-FKEV 474
Cdd:PLN02744 424 GLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVI--PGSGPDqYNFA 501
|
490 500 510
....*....|....*....|....*....|....*...
gi 20129315 475 NMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
85-512 |
7.55e-129 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 381.06 E-value: 7.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 85 LPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCIIVPDQGSVAA 164
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEAEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 165 FAnfkddgaaaapaapaaapapaPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQLRLQG 244
Cdd:PRK11856 86 AA---------------------AEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLST 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 245 -KGSGVHGSIKSGDL----AGQKAAAKPAAAAPAKAPRAAGARYEDIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQVDK 319
Cdd:PRK11856 145 vKGSGPGGRITKEDVeaaaAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 320 LLKFRAKVNKKYEKqgarVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVFNADRKGVL 399
Cdd:PRK11856 225 LLALRKQLKAIGVK----LTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 400 EISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPDSlkgFKEVNMLTV 479
Cdd:PRK11856 301 ELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE---IVVRKVMPL 377
|
410 420 430
....*....|....*....|....*....|...
gi 20129315 480 TLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PRK11856 378 SLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
299-510 |
3.36e-91 |
|
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: 277.12 E-value: 3.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 299 LLESKTQLPHYYVTVQCQVDKLLKFRAKVNKKYEKQGARVSVNDFIIKAVAIASLKVPEANSAWMDT--VIRKYDDVDVS 376
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 377 VAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGT 456
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 20129315 457 TTKQLVADPDslkGFKEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNM 510
Cdd:pfam00198 161 IRKRPVVVDG---EIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
95-512 |
1.02e-62 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 213.92 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 95 GSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCIIVPDQGSVAAFAnfkddgaa 174
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAA-------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 175 aapaapaaapaPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQLRL-QGKGSGVHGSI 253
Cdd:PRK11855 204 -----------APAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLsQVKGTGKKGRI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 254 KSGDLAGQKAAAKPAAAAPAKAPRAAGAR-----------------YEDIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQ 316
Cdd:PRK11855 273 TKEDVQAFVKGAMSAAAAAAAAAAAAGGGglgllpwpkvdfskfgeIETKPLSRIKKISAANLHRSWVTIPHVTQFDEAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 317 VDKLLKFRAKVNKKYEKQGARVSVNDFIIKAVAIASLKVPEANS---AWMDTVIRKyDDVDVSVAVSTDKGLITPIVFNA 393
Cdd:PRK11855 353 ITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNAsldEDGDELTYK-KYFNIGFAVDTPNGLVVPVIKDV 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 394 DRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPDSlkgFKE 473
Cdd:PRK11855 432 DKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKE---FVP 508
|
410 420 430
....*....|....*....|....*....|....*....
gi 20129315 474 VNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PRK11855 509 RLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
81-512 |
1.64e-57 |
|
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: 196.49 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 81 IRVPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCII----V 156
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILeegnD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 157 PDQGSVAAFANFKDDGAAAAPAAPAAAPAPapaaaaapppppppaaapaaaapppapaaapaaagtgRVYASPMAKRLAE 236
Cdd:TIGR01347 80 ATAAPPAKSGEEKEETPAASAAAAPTAAAN-------------------------------------RPSLSPAARRLAK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 237 AQQLRL-QGKGSGVHGSIKSGDLAGQKAAAKPAAAAPAKAPRAAGARY----EDIPVTNMRAVIAKRLLESKTQLPhyYV 311
Cdd:TIGR01347 123 EHGIDLsAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAAtrpeERVKMTRLRQRIAERLKEAQNSTA--ML 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 312 TVQCQVD--KLLKFRAKVNKKYEKQ-GARVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITP 388
Cdd:TIGR01347 201 TTFNEVDmsAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 389 IVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPDSl 468
Cdd:TIGR01347 281 VVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQ- 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 20129315 469 kgFKEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:TIGR01347 360 --IEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
31-512 |
4.17e-51 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 179.88 E-value: 4.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 31 STGNVVVRALSSQLINSRKLQSIRSKLNtsQSPVTWSYNFARAYANLPehirVPLPALSPTMERGSIVSWEKKEGDKLNE 110
Cdd:PTZ00144 1 STVNLVKRLNKPLLSSVKGMFRRFSLRK--LQPACSAHFSKSYFSIKV----IKVPTMGDSISEGTVVEWKKKVGDYVKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 111 GDLLCEIETDKATMGFETPEEGFLAKILIQGGTkDVPVGQLLCIIVPD-QGSVAAFANFKDDGAAAAPAAPAAAPAPAPA 189
Cdd:PTZ00144 75 DEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEIDTGgAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 190 AAAAPPPPPPPAAApaaaapppapaaapaaagtgRVYASPMAKRLAEAQQLRLQGKGSgvhgsiksgdlagqkaaakpaa 269
Cdd:PTZ00144 154 PPAASKPTPPAAAK--------------------PPEPAPAAKPPPTPVARADPRETR---------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 270 aapakapraagaryedIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQVDKLLKFRAKVNKKYEKQ-GARVSVNDFIIKAV 348
Cdd:PTZ00144 192 ----------------VPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKAS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 349 AIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTIS 428
Cdd:PTZ00144 256 TIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 429 VSNLGMFGVNQFAAVINPPQSCILAIGTTTK-------QLVADPdslkgfkevnMLTVTLSADHRVVDGAVAARWLQHFR 501
Cdd:PTZ00144 336 ISNGGVFGSLMGTPIINPPQSAILGMHAIKKrpvvvgnEIVIRP----------IMYLALTYDHRLIDGRDAVTFLKKIK 405
|
490
....*....|.
gi 20129315 502 DYMEDPSNMVL 512
Cdd:PTZ00144 406 DLIEDPARMLL 416
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
81-512 |
5.20e-51 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 179.26 E-value: 5.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 81 IRVPlpALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTkDVPVGQLLCIIVPDQG 160
Cdd:PRK05704 5 IKVP--TLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 161 SVAAFAnfkddgaaaapaapaaapapapaaaaappppppPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQL 240
Cdd:PRK05704 82 AGAAAA---------------------------------AAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 241 RL-QGKGSGVHGSIKSGDLAGQKAAAKPAAAAPAKAPRAAGARYED------IPVTNMRAVIAKRLLESKTQ---Lphyy 310
Cdd:PRK05704 129 DAsAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGarpeerVPMTRLRKTIAERLLEAQNTtamL---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 311 vTVQCQVD--KLLKFRAKVNKKYEKQ-GARVSVNDFIIKAVaIASLK-VPEANsAWMD---TVIRKYddVDVSVAVSTDK 383
Cdd:PRK05704 205 -TTFNEVDmtPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAV-VEALKrYPEVN-ASIDgddIVYHNY--YDIGIAVGTPR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 384 GLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVA 463
Cdd:PRK05704 280 GLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVA 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 20129315 464 dpdslKGFKEVN--MLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PRK05704 360 -----VNGQIVIrpMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
95-512 |
5.74e-47 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 172.88 E-value: 5.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 95 GSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCIIVpDQGSVAAFANFKDDgaa 174
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFE-VEGAAPAAAPAKQE--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 175 aapaapaaapapapaaAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQLRLQG-KGSGVHGSI 253
Cdd:PRK11854 294 ----------------AAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKvKGTGRKGRI 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 254 KSGDLAGQKAAAKPAAAAPAKAPRAAGARY----------------EDIPVTNMRAVIAKRLLESKTQLPHyyVTvqcQV 317
Cdd:PRK11854 358 LKEDVQAYVKDAVKRAEAAPAAAAAGGGGPgllpwpkvdfskfgeiEEVELGRIQKISGANLHRNWVMIPH--VT---QF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 318 DK-----LLKFRAKVNKKYEKQ--GARVSVNDFIIKAVAIASLKVPEANSAWMD---TVIRKyDDVDVSVAVSTDKGLIT 387
Cdd:PRK11854 433 DKaditeLEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEdgqRLTLK-KYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 388 PIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVadpDS 467
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPV---WN 588
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 20129315 468 LKGFKEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PRK11854 589 GKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
222-512 |
1.03e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 160.84 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 222 TGRVYASPMAKRLAEAQQLRLQG-KGSGVHGSIKSGDLAGQKAAAKPAAAAPAKAPRAAGARYED----------IPVTN 290
Cdd:PRK14843 46 TNVVRISPLAKRIALEHNIAWQEiQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDnvtpygeierIPMTP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 291 MRAVIAKRLLESKTQLPHYYVTVQCQVDKLLKFRAKV-NKKYEKQGARVSVNDFIIKAVAIASLKVPEANSAWMD--TVI 367
Cdd:PRK14843 126 MRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVlEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEdgKTI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 368 RKYDDVDVSVAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPP 447
Cdd:PRK14843 206 ITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQP 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129315 448 QSCILAIGTTtkqlVADPDSLKGFKEVN-MLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PRK14843 286 NSAILGVSST----IEKPVVVNGEIVIRpIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
93-512 |
2.85e-44 |
|
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: 163.89 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 93 ERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCIIvpdQGSVAAFAnfkddg 172
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTL---SVAGSTPA------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 173 aaaapAAPAAAPAPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGTGRVYASPMAKRLAEAQQLRLQG-KGSGVHG 251
Cdd:TIGR01348 198 -----TAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAvKGTGIKG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 252 SIKSGDLAGQKAAAKPAAAAPAKAPRAAGARY--------------EDIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQV 317
Cdd:TIGR01348 273 RILREDVQRFVKEPSVRAQAAAASAAGGAPGAlpwpnvdfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 318 DKLLKFRAKVNKKYEKQGARVSVNDFIIKAVAIASLKVPEANSAWMDT----VIRKYddVDVSVAVSTDKGLITPIVFNA 393
Cdd:TIGR01348 353 TEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGgeqlILKKY--VNIGVAVDTPNGLLVPVIKDV 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 394 DRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPdslKGFKE 473
Cdd:TIGR01348 431 DRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNG---KEFEP 507
|
410 420 430
....*....|....*....|....*....|....*....
gi 20129315 474 VNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:TIGR01348 508 RLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
97-512 |
1.06e-37 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 143.32 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 97 IVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKIliQGGTKD-VPVGQ-LLCIIVPDQGSVAAFANFKDDGAA 174
Cdd:PLN02528 15 LLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQI--NFSPGDiVKVGEtLLKIMVEDSQHLRSDSLLLPTDSS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 175 AAPAAPAAAPAPAPaaaaapppppppaaapaaaapppapaaapaaagTGRVYASPMAKRLAEAQQLRLqgkgSGVHGSIK 254
Cdd:PLN02528 93 NIVSLAESDERGSN---------------------------------LSGVLSTPAVRHLAKQYGIDL----NDILGTGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 255 SG-------------------DLAGQKAAAKPAAAAPAKAPRAAGARYED--IPVTNMRAVIAKRLLESkTQLPHYYVTV 313
Cdd:PLN02528 136 DGrvlkedvlkyaaqkgvvkdSSSAEEATIAEQEEFSTSVSTPTEQSYEDktIPLRGFQRAMVKTMTAA-AKVPHFHYVE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 314 QCQVDKLLKFRAKVNKKYEKQGARVSVNDFIIKAVAIASLKVPEANSAWMDTV--IRKYDDVDVSVAVSTDKGLITPIVF 391
Cdd:PLN02528 215 EINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETseIRLKGSHNIGVAMATEHGLVVPNIK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 392 NADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKqlVADPDSLKGF 471
Cdd:PLN02528 295 NVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNV 372
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 20129315 472 KEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PLN02528 373 YPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
286-512 |
2.83e-30 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 123.33 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 286 IPVTNMRAVIAKRLLESKTQLPHYYVTVQCQVDKLLKFRAKVNKK-YEKQGARVSVNDFIIKAVAIASLKVPEANSAWMD 364
Cdd:PLN02226 237 VPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 365 TVIRKYDDVDVSVAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVI 444
Cdd:PLN02226 317 DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPII 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129315 445 NPPQSCILAIGTttkqLVADPDSLKG-FKEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL 512
Cdd:PLN02226 397 NPPQSAILGMHS----IVSRPMVVGGsVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
83-155 |
7.47e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 105.95 E-value: 7.47e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCII 155
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
224-507 |
1.55e-26 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 109.50 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 224 RVYASPMAKRLAEAQQLRL-QGKGSGVHGSIKSGDLAGQKAAAKPAAAAPAKAPRAAGARYEDIP--------------- 287
Cdd:PRK11857 1 KILATPIARALAKKLGIDIsLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAapaaappklegkrek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 288 VTNMRAVIAKRLLESKTQLPHYYVTVQCQVDKLLKFRAKVNKKYEK-QGARVSVNDFIIKAVAIA-------SLKVPEAN 359
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKtEGVKLTFLPFIAKAILIAlkefpifAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 360 SAwmdtvIRKYDDVDVSVAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQ 439
Cdd:PRK11857 161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129315 440 FAAVINPPQSCILAIGT-TTKQLVADPDSLKGfkevNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDP 507
Cdd:PRK11857 236 GVPVINYPELAIAGVGAiIDKAIVKNGQIVAG----KVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
81-166 |
4.41e-25 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 107.70 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 81 IRVPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKDVPVGQLLCIIVPDQG 160
Cdd:PRK11892 3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGE 82
|
....*.
gi 20129315 161 SVAAFA 166
Cdd:PRK11892 83 SASDAG 88
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
83-156 |
2.13e-23 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 93.59 E-value: 2.13e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCIIV 156
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
83-155 |
4.05e-18 |
|
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: 78.64 E-value: 4.05e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129315 83 VPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCII 155
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
85-166 |
1.36e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.53 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 85 LPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTkDVPVGQLLCIIVPDQGS--- 161
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEVSdae 85
|
....*....
gi 20129315 162 ----VAAFA 166
Cdd:PRK14875 86 idafIAPFA 94
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
83-155 |
1.61e-14 |
|
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: 68.40 E-value: 1.61e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129315 83 VPLPALSPTMERGsIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKdVPVGQLLCII 155
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
80-155 |
5.59e-06 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 43.94 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 80 HIRVPLPalsptmerGSIVSWEKKEGDKLNEGDLLCEIEtdkaTMGFET----PEEGFLAKILIQGGTKdVPVGQLLCII 155
Cdd:cd06850 1 EVTAPMP--------GTVVKVLVKEGDKVEAGQPLAVLE----AMKMENevtaPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
385-499 |
8.62e-06 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 48.73 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 385 LITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGT-------- 456
Cdd:PRK12270 226 LVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefq 305
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 20129315 457 -TTKQLVADpdslKGFKEVnmLTVTLSADHRVVDGAVAARWLQH 499
Cdd:PRK12270 306 gASEERLAE----LGISKV--MTLTSTYDHRIIQGAESGEFLRT 343
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
225-258 |
6.46e-03 |
|
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: 34.58 E-value: 6.46e-03
10 20 30
....*....|....*....|....*....|....*
gi 20129315 225 VYASPMAKRLAEAQQLRLQG-KGSGVHGSIKSGDL 258
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDvKGTGPGGRITKEDV 35
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
78-155 |
8.59e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 38.91 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129315 78 PEHIRVPLPalsptmerGSIVSWEKKEGDKLNEGDLLCEIEtdkaTMGFET----PEEGFLAKILIQGGTKdVPVGQLLC 153
Cdd:COG1038 1076 PGHIGAPMP--------GTVVKVLVKEGDEVKKGDPLLTIE----AMKMETtitaPRDGTVKEVLVKEGDQ-VEAGDLLI 1142
|
..
gi 20129315 154 II 155
Cdd:COG1038 1143 EL 1144
|
|
| |
