|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
211-632 |
0e+00 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 622.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 211 IVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKQEDI 290
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 291 A-AFADYRPTEVTSLKPQAPPPV---PPPVAAVPPIPQPLAPTPSA----APAGPKGRVFVSPLAKKLAAEKGIDLTQVK 362
Cdd:TIGR01349 82 AdAFKNYKLESSASPAPKPSEIAptaPPSAPKPSPAPQKQSPEPSSpaplSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 363 GTGPEGRIIKKDIDSFVPTKA----APAAAAAAPPGPRVAPTPAGVFIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVN 438
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPasanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 439 MGEVLLVRKELNKMLEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 518
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 519 LETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LIPADNEKGFDVASVM 597
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401
|
410 420 430
....*....|....*....|....*....|....*
gi 78365255 598 SVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
202-632 |
3.76e-169 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 493.22 E-value: 3.76e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 202 GSSYPVHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 281
Cdd:PLN02744 106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 282 IIVEKQEDIAAFADYRPTEVTSLKPQAPPPVPPPVAAVPPIPQPLAPTPSA----APAGPKGRVFVSPLAKKLAAEKGID 357
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKAskpsAPPSSGDRIFASPLARKLAEDNNVP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 358 LTQVKGTGPEGRIIKKDIDSFVptkaAPAAAAAAPPGPRVAPTPAGVFIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDV 437
Cdd:PLN02744 266 LSSIKGTGPDGRIVKADIEDYL----ASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDT 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 438 NMGEVLLVRKELNKMLE--GKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAH 515
Cdd:PLN02744 342 RVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDAD 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 516 IKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVA 594
Cdd:PLN02744 422 KKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNFA 501
|
410 420 430
....*....|....*....|....*....|....*...
gi 78365255 595 SVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
421-631 |
2.60e-93 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 286.36 E-value: 2.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 421 LMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKG-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 497
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 498 VAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 577
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 78365255 578 SEDKLIPADNEkgFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTML 631
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
209-283 |
8.41e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.86 E-value: 8.41e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78365255 209 MQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 283
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
87-166 |
7.27e-24 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 105.00 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 87 LPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEA 166
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
83-156 |
2.84e-23 |
|
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: 93.62 E-value: 2.84e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78365255 83 QKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIICI 156
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
210-284 |
2.26e-20 |
|
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: 85.50 E-value: 2.26e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78365255 210 QIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 284
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
85-156 |
2.99e-19 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 82.04 E-value: 2.99e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78365255 85 VPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTrDVPVGSIICI 156
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
85-156 |
1.41e-10 |
|
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: 57.61 E-value: 1.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78365255 85 VPLPSLSPTMQAGtIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIICI 156
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
211-632 |
0e+00 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 622.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 211 IVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKQEDI 290
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 291 A-AFADYRPTEVTSLKPQAPPPV---PPPVAAVPPIPQPLAPTPSA----APAGPKGRVFVSPLAKKLAAEKGIDLTQVK 362
Cdd:TIGR01349 82 AdAFKNYKLESSASPAPKPSEIAptaPPSAPKPSPAPQKQSPEPSSpaplSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 363 GTGPEGRIIKKDIDSFVPTKA----APAAAAAAPPGPRVAPTPAGVFIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVN 438
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPasanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 439 MGEVLLVRKELNKMLEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 518
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 519 LETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LIPADNEKGFDVASVM 597
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401
|
410 420 430
....*....|....*....|....*....|....*
gi 78365255 598 SVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
202-632 |
3.76e-169 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 493.22 E-value: 3.76e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 202 GSSYPVHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 281
Cdd:PLN02744 106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 282 IIVEKQEDIAAFADYRPTEVTSLKPQAPPPVPPPVAAVPPIPQPLAPTPSA----APAGPKGRVFVSPLAKKLAAEKGID 357
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKAskpsAPPSSGDRIFASPLARKLAEDNNVP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 358 LTQVKGTGPEGRIIKKDIDSFVptkaAPAAAAAAPPGPRVAPTPAGVFIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDV 437
Cdd:PLN02744 266 LSSIKGTGPDGRIVKADIEDYL----ASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDT 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 438 NMGEVLLVRKELNKMLE--GKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAH 515
Cdd:PLN02744 342 RVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDAD 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 516 IKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVA 594
Cdd:PLN02744 422 KKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNFA 501
|
410 420 430
....*....|....*....|....*....|....*...
gi 78365255 595 SVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
210-632 |
2.76e-151 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 442.69 E-value: 2.76e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 210 QIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKQED 289
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 290 IAAFADYRPTEVTSlkpqapppvPPPVAAVPPIPQPLAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGR 369
Cdd:PRK11856 83 EAAAAAEAAPEAPA---------PEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 370 IIKKDIDSFVPTKAAPAAAAAAPPGPRVAPTPAGVfIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKEL 449
Cdd:PRK11856 154 ITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAEGE-ERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 450 NkmlEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSL 529
Cdd:PRK11856 233 K---AIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 530 ASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEkgFDVASVMSVTLSCDHRVVD 609
Cdd:PRK11856 310 AEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMPLSLSFDHRVID 387
|
410 420
....*....|....*....|...
gi 78365255 610 GAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PRK11856 388 GADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
421-631 |
2.60e-93 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 286.36 E-value: 2.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 421 LMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKG-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 497
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 498 VAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 577
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 78365255 578 SEDKLIPADNEkgFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTML 631
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
97-632 |
7.56e-87 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 281.33 E-value: 7.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 97 GTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGS-IICITVEKPQDIEAfknyTLDSA 175
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGlLAVIEAAGAAAAAA----APAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 176 TAATQAAPAPAAAPAAAPAAPSASAPGSSYPVHMqivlPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfE 255
Cdd:PRK11855 91 AAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKV----PDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATM--E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 256 V--QEEGYLAKILVPEGTRdVPLGTPLcIIVEKQEDIAAFADYRPTEVTSlkpqapPPVPPPVAAVPPIPQPLAPTPSAA 333
Cdd:PRK11855 164 IpsPVAGVVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAAAPAAAAPA------AAAAAAPAPAPAAAAAPAAAAPAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 334 PAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFV------PTKAAPAAAAAAPPGPRVAPTPAGVFID 407
Cdd:PRK11855 236 AAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVkgamsaAAAAAAAAAAAGGGGLGLLPWPKVDFSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 408 ------IPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKG-KISVNDFIIKASALACLKVPEAN 480
Cdd:PRK11855 316 fgeietKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGvKLTMLPFFIKAVVAALKEFPVFN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 481 SSWMDT---VIRQNHvVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFG 557
Cdd:PRK11855 396 ASLDEDgdeLTYKKY-FNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78365255 558 IKNFSAIINPPQACILAIGASEDKliPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PRK11855 475 GTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
211-632 |
3.04e-72 |
|
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: 238.48 E-value: 3.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 211 IVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEkqedi 290
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 291 AAFADYRPTEVTSLKPQapppvpppvaavppipQPLAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRI 370
Cdd:TIGR01347 77 GNDATAAPPAKSGEEKE----------------ETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 371 IKKDIDSFVPTKAAPAAAAAAPPGPRVAPTPAGVfIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELN 450
Cdd:TIGR01347 141 TKEDIIKKTEAPASAQPPAAAAAAAAPAAATRPE-ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 451 KMLEGKG--KISVNDFIIKASALACLKVPEANSSwmdtvIRQNHVV-----DVSVAVSTPAGLITPIVFNAHIKGLETIA 523
Cdd:TIGR01347 220 EEFEKKHgvKLGFMSFFVKAVVAALKRFPEVNAE-----IDGDDIVykdyyDISVAVSTDRGLVVPVVRNADRMSFADIE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 524 SDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIpADNEKgFDVASVMSVTLSC 603
Cdd:TIGR01347 295 KEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIRPMMYLALSY 372
|
410 420
....*....|....*....|....*....
gi 78365255 604 DHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:TIGR01347 373 DHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
211-632 |
4.93e-65 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 219.32 E-value: 4.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 211 IVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTrDVPLGTPLCIIVEKQE 288
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 289 DIAAFADYRPTEVTslkpqapppvpppvaavppipQPLAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEG 368
Cdd:PRK05704 82 AGAAAAAAAAAAAA---------------------AAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 369 RIIKKDIDSFV-PTKAAPAAAAAAPPGPRVAPTPAGVFIDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRK 447
Cdd:PRK05704 141 RVTKEDVLAALaAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 448 ELNKMLEGK-----GKISvndFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETI 522
Cdd:PRK05704 221 QYKDAFEKKhgvklGFMS---FFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 523 ASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEkgFDVASVMSVTLS 602
Cdd:PRK05704 298 EKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPMMYLALS 375
|
410 420 430
....*....|....*....|....*....|..
gi 78365255 603 CDHRVVDG--AVGaqWLAEFKKYLEKPVTMLL 632
Cdd:PRK05704 376 YDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
211-632 |
2.55e-62 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 212.62 E-value: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 211 IVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIvekqeDI 290
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEI-----DT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 291 AAFADYRPTEVTSLKPQAPPPVPPPVAAVPPIPQPLAPTPSAAPAGPKgrVFVSPLAKKLAaekgidlTQVKGTGPEGRi 370
Cdd:PTZ00144 121 GGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKP--PEPAPAAKPPP-------TPVARADPRET- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 371 ikkdidsfvptkaapaaaaaappgprvaptpagvfiDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELN 450
Cdd:PTZ00144 191 ------------------------------------RVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 451 KMLEGKG--KISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVS 528
Cdd:PTZ00144 235 DDFQKKHgvKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 529 LASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEkgFDVASVMSVTLSCDHRVV 608
Cdd:PTZ00144 315 LAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYLALTYDHRLI 392
|
410 420
....*....|....*....|....
gi 78365255 609 DGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PTZ00144 393 DGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
85-625 |
8.21e-62 |
|
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: 215.26 E-value: 8.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 85 VPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEgTRDVPVGSIICI---TVEKP 161
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIigePGEAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 162 QDIEAFKNYTLDSATAATQAAPAPAAAPAAAPAAPSASAPGSSYPVHMqivlPALSPTMTMGTVQRWEKKVGEKLSEGDL 241
Cdd:TIGR02927 84 SEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKM----PELGESVTEGTVTSWLKAVGDTVEVDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 242 LAEIETDKATIGFEVQEEGYLAKILVPEgTRDVPLGTPLCII--------VEKQEDIAAFADYRPTEVTSLKPQAPPPVP 313
Cdd:TIGR02927 160 LLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIgdanaapaEPAEEEAPAPSEAGSEPAPDPAARAPHAAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 314 PPVAAVPPIPQPLAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPTKAAPAAAAAAPP 393
Cdd:TIGR02927 239 DPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 394 GPRVAPTPAGVFIDI------------PISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKEL-NKMLEGKG-KI 459
Cdd:TIGR02927 319 AAAAPAAPAAAAKPAepdtaklrgttqKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAkNDFLEKNGvNL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 460 SVNDFIIKASALACLKVPEANSSWMDTV--IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGK 537
Cdd:TIGR02927 399 TFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 538 LQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVASVMSVT---LSCDHRVVDGAVGA 614
Cdd:TIGR02927 479 LKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLVDGADAG 558
|
570
....*....|.
gi 78365255 615 QWLAEFKKYLE 625
Cdd:TIGR02927 559 RFLTTIKKRLE 569
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
341-632 |
2.82e-59 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 202.06 E-value: 2.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 341 VFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPTKAAPAAAAAAPPGPRVA-----PTPAGVFIDIPISNIRR 415
Cdd:PRK14843 49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEevpdnVTPYGEIERIPMTPMRK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 416 VIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKE-LNKMLEGKGK-ISVNDFIIKASALACLKVPEANSSWMD---TVIRQ 490
Cdd:PRK14843 129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKkTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 491 NHVvDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQA 570
Cdd:PRK14843 209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78365255 571 CILAIGASEDKLIPADNEkgFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PRK14843 288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
97-632 |
5.76e-57 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 203.31 E-value: 5.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 97 GTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIIcITVEKPQDIEAfknytldsat 176
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VSTGSLI-MVFEVAGEAPA---------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 177 aatqaapAPAAAPAAAPAAPSASAPGSSYPVHMqivlPALSptMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEV 256
Cdd:PRK11854 186 -------AAPAAAEAAAPAAAPAAAAGVKDVNV----PDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 257 QEEGYLAKILVPEGTRdVPLGTpLCIIVEKQEDIAAFADYRPTEVTSlkpqapppvpppvAAVPPIPQPLAPTPSAAPAG 336
Cdd:PRK11854 253 PFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAAPAKQEAAAP-------------APAAAKAEAPAAAPAAKAEG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 337 PKGR------VFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFV--PTKAAPAAAAAAPPGPRVAPTPAGVFID- 407
Cdd:PRK11854 318 KSEFaendayVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVkdAVKRAEAAPAAAAAGGGGPGLLPWPKVDf 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 408 --------IPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKG---KISVNDFIIKASALACLKV 476
Cdd:PRK11854 398 skfgeieeVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKlgvKITPLVFIMKAVAAALEQM 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 477 PEANSSWMD---TVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNL 553
Cdd:PRK11854 478 PRFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSI 556
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78365255 554 GMFGIKNFSAIINPPQACILAIGASEDKliPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PRK11854 557 GGLGTTHFTPIVNAPEVAILGVSKSAME--PVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
105-632 |
6.31e-52 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 187.77 E-value: 6.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 105 KEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIICITvekpqDIEAFKNYTLDSATAATQAAPA 184
Cdd:TIGR01348 22 KPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDT-LPVGGVIATL-----EVGAGAQAQAEAKKEAAPAPTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 185 PAAAPAAAPAAPSASAPGSSYpvhMQIVLPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAK 264
Cdd:TIGR01348 96 GAPAPAAQAQAAPAAGQSSGV---QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 265 ILVPEGTRdvpLGTPLCIIVEKQEDIAAFADYRPtevtslkpqapppvpPPVAAVPPIPQPLAPTPSAAPAGPKGR---- 340
Cdd:TIGR01348 172 VKVKVGDS---VPTGDLILTLSVAGSTPATAPAP---------------ASAQPAAQSPAATQPEPAAAPAAAKAQapap 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 341 -----------VFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPTKAAPAAAAAAPPGPRVAPTPA------- 402
Cdd:TIGR01348 234 qqagtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPwpnvdfs 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 403 --GVFIDIPISNIRRVIAQRLMQSKQTIPH--YYLSVDVNMGEVLLVRKELNKMLEGkGKISVNDFIIKASALACLKVPE 478
Cdd:TIGR01348 314 kfGEVEEVDMSRIRKISGANLTRNWTMIPHvtHFDKADITEMEAFRKQQNAAVEKEG-VKLTVLHILMKAVAAALKKFPK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 479 ANSSWM---DTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGM 555
Cdd:TIGR01348 393 FNASLDlggEQLILKKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGG 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78365255 556 FGIKNFSAIINPPQACILaiGASEDKLIPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:TIGR01348 472 IGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
227-632 |
1.08e-50 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 181.07 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 227 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGtrD-VPLGTPLCIIVEKQEDIAAFADYRPTEVTSLK 305
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DiVKVGETLLKIMVEDSQHLRSDSLLLPTDSSNI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 306 PQAPPpvpppvaavppipqplaptpSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPTK--- 382
Cdd:PLN02528 95 VSLAE--------------------SDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKgvv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 383 -----AAPAAAAAAPPGPRVAPTPAG-VFID--IPISNIRRVIAQRlMQSKQTIPHYYLSVDVNMGEVLLVRKELNKM-L 453
Cdd:PLN02528 155 kdsssAEEATIAEQEEFSTSVSTPTEqSYEDktIPLRGFQRAMVKT-MTAAAKVPHFHYVEEINVDALVELKASFQENnT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 454 EGKGKISVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSL 529
Cdd:PLN02528 234 DPTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 530 ASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDklIPADNEKGFDV-ASVMSVTLSCDHRVV 608
Cdd:PLN02528 312 QHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIGADHRVL 389
|
410 420
....*....|....*....|....
gi 78365255 609 DGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PLN02528 390 DGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
340-627 |
8.33e-41 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 150.71 E-value: 8.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 340 RVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFV---PTKAAPAAAAAAPPGPRVAPTPAGVFIDI-------P 409
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslKSAPTPAEAASVSSAQQAAKTAAPAAAPPklegkreK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 410 ISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKE-LNKMLEGKG-KISVNDFIIKASALACLKVP-------EAN 480
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSvKDPVLKTEGvKLTFLPFIAKAILIALKEFPifaakydEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 481 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKN 560
Cdd:PRK11857 161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78365255 561 FSAIINPPQACILAIGASEDKLIPadnEKGFDVAS-VMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKP 627
Cdd:PRK11857 236 GVPVINYPELAIAGVGAIIDKAIV---KNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
209-632 |
7.61e-29 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 120.25 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 209 MQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPlGTPLCIIVEKQE 288
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEP-GTKVAIISKSED 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 289 DIAAFAdyrPTEvtslkpqapppvpppvaavpPIPQPLAPTPSA-APAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPE 367
Cdd:PLN02226 171 AASQVT---PSQ--------------------KIPETTDPKPSPpAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 368 griikkdidsfVPTKAAPAAaaaappgprvaptpagvfidIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRK 447
Cdd:PLN02226 228 -----------LPPKERERR--------------------VPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 448 EL-NKMLEGKG-KISVNDFIIKASALACLKVPEANSSW-MDTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGLETIAS 524
Cdd:PLN02226 277 QYkDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNFAEIEK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 525 DVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKliPADNEKGFDVASVMSVTLSCD 604
Cdd:PLN02226 356 TINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSR--PMVVGGSVVPRPMMYVALTYD 433
|
410 420
....*....|....*....|....*...
gi 78365255 605 HRVVDGAVGAQWLAEFKKYLEKPVTMLL 632
Cdd:PLN02226 434 HRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
210-337 |
2.07e-28 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 118.87 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 210 QIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKQED 289
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 78365255 290 IAAFADYRPTEVTSLKPQAPPPVPPPVAAVPPIPQPLAPTPSAAPAGP 337
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADP 131
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
209-283 |
8.41e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.86 E-value: 8.41e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78365255 209 MQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 283
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
87-166 |
7.27e-24 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 105.00 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 87 LPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEA 166
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
210-283 |
1.96e-23 |
|
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: 94.05 E-value: 1.96e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78365255 210 QIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 283
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
83-156 |
2.84e-23 |
|
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: 93.62 E-value: 2.84e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78365255 83 QKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIICI 156
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
210-284 |
2.26e-20 |
|
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: 85.50 E-value: 2.26e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78365255 210 QIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 284
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
85-156 |
2.99e-19 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 82.04 E-value: 2.99e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78365255 85 VPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTrDVPVGSIICI 156
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
85-156 |
2.03e-15 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 71.32 E-value: 2.03e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78365255 85 VPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIICI 156
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVK 72
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
341-376 |
6.90e-15 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 68.48 E-value: 6.90e-15
10 20 30
....*....|....*....|....*....|....*.
gi 78365255 341 VFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDID 376
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
211-375 |
2.29e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 71.90 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 211 IVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEkqedi 290
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVAD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 291 aafadyrptevtslkpqapppvpppvaavppipqplAPTPSAApagpkGRVFVSPLAKKLAAEkGIDLTQVKGTGPEGRI 370
Cdd:PRK14875 79 ------------------------------------AEVSDAE-----IDAFIAPFARRFAPE-GIDEEDAGPAPRKARI 116
|
....*
gi 78365255 371 IKKDI 375
Cdd:PRK14875 117 GGRTV 121
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
83-167 |
6.67e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 70.74 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 83 QKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTrDVPVGSIICITVEK-- 160
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAev 81
|
....*...
gi 78365255 161 -PQDIEAF 167
Cdd:PRK14875 82 sDAEIDAF 89
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
210-283 |
8.62e-12 |
|
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: 61.08 E-value: 8.62e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78365255 210 QIVLPALSPTMTMGTVQrWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 283
Cdd:pfam00364 2 EIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
85-156 |
1.41e-10 |
|
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: 57.61 E-value: 1.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78365255 85 VPLPSLSPTMQAGtIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRdVPVGSIICI 156
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
293-624 |
4.95e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 52.97 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 293 FADYRPTEVTSLKPQAPPPVPPPVAAVPPIPQP----------------LAPTPSAAPAGPKGRVFVSPLAKKLA-AEKG 355
Cdd:PRK12270 33 FADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKapaapapappaaaapaAPPKPAAAAAAAAAPAAPPAAAAAAApAAAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 356 IDLTQVKGTGPEGRIIKKDIDSF-VPTkaapaaaaaappgprvaPT-----PAGVFIDipisNiRRVIAQRLMQSKQtip 429
Cdd:PRK12270 113 VEDEVTPLRGAAAAVAKNMDASLeVPT-----------------ATsvravPAKLLID----N-RIVINNHLKRTRG--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 430 hyylsvdvnmgevllvrkelnkmlegkGKISVNDFIIKASALACLKVPEANSSWMD-----TVIRQNHV-VDVSVAVSTP 503
Cdd:PRK12270 168 ---------------------------GKVSFTHLIGYALVQALKAFPNMNRHYAEvdgkpTLVTPAHVnLGLAIDLPKK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78365255 504 AGLITPIVfnAHIKGLETIA--------SDVVSlasKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAI 575
Cdd:PRK12270 221 DGSRQLVV--PAIKGAETMDfaqfwaayEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 78365255 576 GA----------SEDKLipadNEKGfdVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYL 624
Cdd:PRK12270 296 GAmeypaefqgaSEERL----AELG--ISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
223-283 |
1.24e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 37.78 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78365255 223 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 283
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
|
|
| |
