|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
213-645 |
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: 582.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 213 KIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRDVPLGAPLCIIVEKESD 292
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 293 I-GAFKDY-VETGVGDVSMPPPAPAPTPVTLQAPVPSAA------PAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQV 364
Cdd:TIGR01349 81 VaDAFKNYkLESSASPAPKPSEIAPTAPPSAPKPSPAPQkqspepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 365 SGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAAPAAAAAApaapaGTFTDIPISNIRKVIAQRLMQSKQTIPHYY 444
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVST-----GSYEDVPLSNIRKIIAKRLLESKQTIPHYY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 445 LSVDVNMDQVLELRKELNeevkAQN---IKLSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLIT 521
Cdd:TIGR01349 236 VSIECNVDKLLALRKELN----AMAsevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 522 PIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKR-LMPADN 600
Cdd:TIGR01349 312 PIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDE 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 961897783 601 EKGFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:TIGR01349 392 EKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
209-645 |
7.72e-164 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 480.12 E-value: 7.72e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 209 PPHMKIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRDVPLGAPLCIIVE 288
Cdd:PLN02744 110 PPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 289 KESDIGAFKDYVETGVGDV----SMPPPAPAPTPVTLQAPVPSAAPAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQV 364
Cdd:PLN02744 190 EEEDIGKFKDYKPSSSAAPaapkAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 365 SGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAApaaaaaapaapagTFTDIPISNIRKVIAQRLMQSKQTIPHYY 444
Cdd:PLN02744 270 KGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL-------------DYTDIPNTQIRKVTASRLLQSKQTIPHYY 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 445 LSVDVNMDQVLELRKELNEEVKAQNIK-LSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLITPI 523
Cdd:PLN02744 337 LTVDTRVDKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 524 VFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNL-GMFGVKNFSAIINPPQACILAVGGSEKRLMPADNEK 602
Cdd:PLN02744 417 VKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPD 496
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 961897783 603 GFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PLN02744 497 QYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
433-644 |
4.82e-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: 285.98 E-value: 4.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 433 LMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKAQNIKLSVNDFIIKASALACLKVPECNSSWMDT--VIRQNHVVDVS 510
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 511 VAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGG 590
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 961897783 591 SEKRlmPADNEKGFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTML 644
Cdd:pfam00198 161 IRKR--PVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
86-157 |
8.10e-26 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 111.16 E-value: 8.10e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRDVNVGSVICI 157
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAV 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
84-157 |
9.77e-24 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 94.78 E-value: 9.77e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961897783 84 QKVELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRdVNVGSVICI 157
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
212-286 |
2.17e-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: 94.01 E-value: 2.17e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961897783 212 MKIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCII 286
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
86-157 |
2.05e-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: 82.81 E-value: 2.05e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTrDVNVGSVICI 157
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
214-287 |
4.17e-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: 81.65 E-value: 4.17e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961897783 214 IALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTrDVPLGAPLCIIV 287
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
86-157 |
5.77e-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: 55.68 E-value: 5.77e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGtIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRdVNVGSVICI 157
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 ... |
213-645 |
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: 582.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 213 KIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRDVPLGAPLCIIVEKESD 292
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 293 I-GAFKDY-VETGVGDVSMPPPAPAPTPVTLQAPVPSAA------PAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQV 364
Cdd:TIGR01349 81 VaDAFKNYkLESSASPAPKPSEIAPTAPPSAPKPSPAPQkqspepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 365 SGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAAPAAAAAApaapaGTFTDIPISNIRKVIAQRLMQSKQTIPHYY 444
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVST-----GSYEDVPLSNIRKIIAKRLLESKQTIPHYY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 445 LSVDVNMDQVLELRKELNeevkAQN---IKLSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLIT 521
Cdd:TIGR01349 236 VSIECNVDKLLALRKELN----AMAsevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 522 PIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKR-LMPADN 600
Cdd:TIGR01349 312 PIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDE 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 961897783 601 EKGFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:TIGR01349 392 EKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
209-645 |
7.72e-164 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 480.12 E-value: 7.72e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 209 PPHMKIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRDVPLGAPLCIIVE 288
Cdd:PLN02744 110 PPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 289 KESDIGAFKDYVETGVGDV----SMPPPAPAPTPVTLQAPVPSAAPAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQV 364
Cdd:PLN02744 190 EEEDIGKFKDYKPSSSAAPaapkAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 365 SGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAApaaaaaapaapagTFTDIPISNIRKVIAQRLMQSKQTIPHYY 444
Cdd:PLN02744 270 KGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL-------------DYTDIPNTQIRKVTASRLLQSKQTIPHYY 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 445 LSVDVNMDQVLELRKELNEEVKAQNIK-LSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLITPI 523
Cdd:PLN02744 337 LTVDTRVDKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 524 VFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNL-GMFGVKNFSAIINPPQACILAVGGSEKRLMPADNEK 602
Cdd:PLN02744 417 VKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPD 496
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 961897783 603 GFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PLN02744 497 QYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
213-645 |
4.19e-146 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 429.98 E-value: 4.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 213 KIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCII-VEKES 291
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIeEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 292 DIGAFKDYVETGVGDVSMPPPAPAPTPVTlqapvpsaapAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQVSGSGPDG 371
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAP----------AAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 372 RITRKDIESFVPPkvapsaaaapSPAAARAAPAAAAAAPAAPAGTFTDIPISNIRKVIAQRLMQSKQTIPHYYLSVDVNM 451
Cdd:PRK11856 153 RITKEDVEAAAAA----------AAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 452 DQVLELRKELneevKAQNIKLSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLITPIVFNAHIKG 531
Cdd:PRK11856 223 TALLALRKQL----KAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 532 LTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRLMPADNEkgFDVSSVMS 611
Cdd:PRK11856 299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMP 376
|
410 420 430
....*....|....*....|....*....|....
gi 961897783 612 VTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PRK11856 377 LSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
433-644 |
4.82e-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: 285.98 E-value: 4.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 433 LMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKAQNIKLSVNDFIIKASALACLKVPECNSSWMDT--VIRQNHVVDVS 510
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 511 VAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGG 590
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 961897783 591 SEKRlmPADNEKGFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTML 644
Cdd:pfam00198 161 IRKR--PVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
98-645 |
2.12e-82 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 269.77 E-value: 2.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 98 GTIARWEKKEGDKISEGDLIAEVETDKATV-------GFemleecyLAKILVPEGTRdVNVGSVIcITVDnpelIPAFKD 170
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMeipspaaGV-------VKEIKVKVGDT-VSVGGLL-AVIE----AAGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 171 ATLESVKSVGAAPSSAASAPPPPSPATAPPPAAPGSSYPphmkIALPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIET 250
Cdd:PRK11855 83 AAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVE----VKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 251 DKATIgfEV--QEEGYLAKILISEGTRdVPLGAPLcIIVEKESDIGAFKDyVETGVGDVSMPPPAPAPTPVTlqapvPSA 328
Cdd:PRK11855 158 DKATM--EIpsPVAGVVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAA-APAAAAPAAAAAAAPAPAPAA-----AAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 329 APAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAAPAAAAA 408
Cdd:PRK11855 228 PAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLLP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 409 APAAPAGTFTDI---PISNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKAQNIKLSVNDFIIKASALA 485
Cdd:PRK11855 308 WPKVDFSKFGEIetkPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 486 CLKVPECNSSWMDT---VIRQNHvVDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFT 562
Cdd:PRK11855 388 LKEFPVFNASLDEDgdeLTYKKY-FNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 563 ISNLGMFGVKNFSAIINPPQACILAVGGSEKRlmPADNEKGFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVT 642
Cdd:PRK11855 467 ISSLGGIGGTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRR 544
|
...
gi 961897783 643 MLL 645
Cdd:PRK11855 545 MLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
214-645 |
3.98e-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: 3.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 214 IALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCIIVEkesdi 293
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 294 gafkdyvETGVGDVSMPPPAPAPTPVTLQAPVPSAAPAAAaapatprkgRVFASPLAKKLAAEKGIDLAQVSGSGPDGRI 373
Cdd:TIGR01347 77 -------GNDATAAPPAKSGEEKEETPAASAAAAPTAAAN---------RPSLSPAARRLAKEHGIDLSAVPGTGVTGRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 374 TRKDIESFvppkvapsaaAAPSPAAARAAPAAAAAAPAAPAGTFTDIPISNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQ 453
Cdd:TIGR01347 141 TKEDIIKK----------TEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 454 VLELRKELNEEV-KAQNIKLSVNDFIIKASALACLKVPECNSSwmdtvIRQNHVV-----DVSVAVSTASGLITPIVFNA 527
Cdd:TIGR01347 211 VMELRKRYKEEFeKKHGVKLGFMSFFVKAVVAALKRFPEVNAE-----IDGDDIVykdyyDISVAVSTDRGLVVPVVRNA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 528 HIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRLMpADNEKgFDVS 607
Cdd:TIGR01347 286 DRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIR 363
|
410 420 430
....*....|....*....|....*....|....*...
gi 961897783 608 SVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:TIGR01347 364 PMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
213-645 |
8.79e-66 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 221.63 E-value: 8.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 213 KIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILISEGTrDVPLGAPLCIIVEke 290
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 291 sdigafkdyvetgvGDVSMPPPAPAPTPVTLQAPVPSAAPAAAAAPATPRkgrvfASPLAKKLAAEKGIDLAQVSGSGPD 370
Cdd:PRK05704 79 --------------GAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-----LSPAARKLAAENGLDASAVKGTGKG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 371 GRITRKDIESFVPPKVAPSAAAAPSPAAARAAPAAAAAAPAapagtftdIPISNIRKVIAQRLMQSKQTIPHYYLSVDVN 450
Cdd:PRK05704 140 GRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEER--------VPMTRLRKTIAERLLEAQNTTAMLTTFNEVD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 451 MDQVLELRKELNEE-VKAQNIKLSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLITPIVFNAHI 529
Cdd:PRK05704 212 MTPVMDLRKQYKDAfEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 530 KGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRLMPADNEkgFDVSSV 609
Cdd:PRK05704 292 LSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPM 369
|
410 420 430
....*....|....*....|....*....|....*...
gi 961897783 610 MSVTLSCDHRVVDG--AVGaqWLAEFRKLLEKPVTMLL 645
Cdd:PRK05704 370 MYLALSYDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
214-645 |
3.37e-58 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 201.83 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 214 IALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTrDVPLGAPLCIIvekesDI 293
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEI-----DT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 294 GAFKDYVETGVGDVSMPPPAPAPTPVTlqapvpsaapaaaaapatprkgrvfASPLAKKLAAEKGIDLAQVsgsgpdgri 373
Cdd:PTZ00144 121 GGAPPAAAPAAAAAAKAEKTTPEKPKA-------------------------AAPTPEPPAASKPTPPAAA--------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 374 tRKDIESFVPPKVAPSAAAAPSpaaaraapaaaaaapaapagTFTDIPISNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQ 453
Cdd:PTZ00144 167 -KPPEPAPAAKPPPTPVARADP--------------------RETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 454 VLELRKELNEEV-KAQNIKLSVNDFIIKASALACLKVPECNSSWMDTVIRQNHVVDVSVAVSTASGLITPIVFNAHIKGL 532
Cdd:PTZ00144 226 LMELRKEYKDDFqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 533 TAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRLMPADNEkgFDVSSVMSV 612
Cdd:PTZ00144 306 AEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYL 383
|
410 420 430
....*....|....*....|....*....|...
gi 961897783 613 TLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PTZ00144 384 ALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
347-645 |
1.33e-56 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 195.12 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 347 SPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAAPAAAAAAPaapaGTFTDIPISNIR 426
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPY----GEIERIPMTPMR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 427 KVIAQRLMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKAQN-IKLSVNDFIIKASALACLKVPECNSSWMD---TVIR 502
Cdd:PRK14843 128 KVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATgKKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIIT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 503 QNHVvDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQ 582
Cdd:PRK14843 208 HNYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPN 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961897783 583 ACILAVGGSEKRLMPADNEkgFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PRK14843 287 SAILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
84-645 |
1.82e-56 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 202.15 E-value: 1.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 84 QKVELPALSPTmqTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRdVNVGSVICItvdnpe 163
Cdd:PRK11854 106 KDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VSTGSLIMV------ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 164 lipaFKDATLESVKSvgaapssaasappppspatapppaapgssyPPHMKIALPALSPTM--------------TMGTVQ 229
Cdd:PRK11854 177 ----FEVAGEAPAAA------------------------------PAAAEAAAPAAAPAAaagvkdvnvpdiggDEVEVT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 230 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGApLCIIVEKESDIGAFKDYVETGVGDVSM 309
Cdd:PRK11854 223 EVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAAPAKQEAAAPAPA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 310 PPPAPAPTPVTLQAPVPSAAPAAAAAPatprkgrVFASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFVPPKVAPS 389
Cdd:PRK11854 301 AAKAEAPAAAPAAKAEGKSEFAENDAY-------VHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 390 AAAAPSPAAARAAPAAAAAAPA--APAGTFTDIPISNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQVLELRKELN--EEV 465
Cdd:PRK11854 374 EAAPAAAAAGGGGPGLLPWPKVdfSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNaeAEK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 466 KAQNIKLSVNDFIIKASALACLKVPECNSSWMD---TVIRQNHVvDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAAL 542
Cdd:PRK11854 454 RKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDI 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 543 AAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRlmPADNEKGFDVSSVMSVTLSCDHRVVD 622
Cdd:PRK11854 533 SKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAME--PVWNGKEFAPRLMLPLSLSYDHRVID 610
|
570 580
....*....|....*....|...
gi 961897783 623 GAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PRK11854 611 GADGARFITIINDRLSDIRRLVL 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
86-638 |
1.98e-56 |
|
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: 201.01 E-value: 1.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 86 VELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEgTRDVNVGSVICITVDNPELI 165
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPGEAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 166 PAFKDATLESVKSVGAAPSSAASAPPPPSPATAPPPAAPGSSYPPhmkIALPALSPTMTMGTVQRWEKKVGEKLSEGDLL 245
Cdd:TIGR02927 84 SEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATE---VKMPELGESVTEGTVTSWLKAVGDTVEVDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 246 AEIETDKATIGFEVQEEGYLAKILISEgTRDVPLGAPLCII--------VEKESDIGAFKDYVETGVGDVSMPPPAPAPT 317
Cdd:TIGR02927 161 LEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIgdanaapaEPAEEEAPAPSEAGSEPAPDPAARAPHAAPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 318 PVTLQAPVPSAAPAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFV-----PPKVAPSAAA 392
Cdd:TIGR02927 240 PPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAkaaeeARAAAAAPAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 393 APSPAAARAAPAAAAAAPAAPAGTFTDIpiSNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKAQN-IK 471
Cdd:TIGR02927 320 AAAPAAPAAAAKPAEPDTAKLRGTTQKM--NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNgVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 472 LSVNDFIIKASALACLKVPECNSSWMDTV--IRQNHVVDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREG 549
Cdd:TIGR02927 398 LTFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 550 KLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRLMPADNEKGFDVSSVMSVT---LSCDHRVVDGAVG 626
Cdd:TIGR02927 478 KLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLVDGADA 557
|
570
....*....|..
gi 961897783 627 AQWLAEFRKLLE 638
Cdd:TIGR02927 558 GRFLTTIKKRLE 569
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
230-645 |
2.68e-55 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 193.78 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 230 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCIIVEKESDIGAFKDYVETGVGDvsm 309
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETLLKIMVEDSQHLRSDSLLLPTDSS--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 310 pppapaptpvtlqapvpSAAPAAAAAPATPRKGRVFASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFVPPKVAPS 389
Cdd:PLN02528 93 -----------------NIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 390 AAAAPSPAAARAAPAAAAAAPAAPAGTFTD--IPISNIRKVIAQRlMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKA 467
Cdd:PLN02528 156 DSSSAEEATIAEQEEFSTSVSTPTEQSYEDktIPLRGFQRAMVKT-MTAAAKVPHFHYVEEINVDALVELKASFQENNTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 468 QNIKLSVNDFIIKASALACLKVPECNSSW----MDTVIRQNHvvDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAALA 543
Cdd:PLN02528 235 PTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 544 AKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKrlMPADNEKGFDV-SSVMSVTLSCDHRVVD 622
Cdd:PLN02528 313 HLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIGADHRVLD 390
|
410 420
....*....|....*....|...
gi 961897783 623 GAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PLN02528 391 GATVARFCNEWKSYVEKPELLML 413
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
346-645 |
2.81e-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: 188.93 E-value: 2.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 346 ASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFVPPKVAPSAAAAPSPAAARAAPAAAAAAPAAPAGTFTDIPISNI 425
Cdd:TIGR01348 247 AAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNVDFSKFGEVEEVDMSRI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 426 RKVIAQRLMQSKQTIPHYYLSVDVNMDQVLELRKELNEEVKAQNIKLSVNDFIIKASALACLKVPECNSSWM---DTVIR 502
Cdd:TIGR01348 327 RKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlggEQLIL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 503 QNHVvDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQ 582
Cdd:TIGR01348 407 KKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPE 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961897783 583 ACILAVggSEKRLMPADNEKGFDVSSVMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:TIGR01348 486 VAILGV--SKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
343-640 |
3.27e-41 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 151.87 E-value: 3.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 343 RVFASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIESFV--PPKVAPSAAAAPSPAAARAAPAAAAAAPAAPAGTFTDi 420
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIksLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 421 PISNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQVLELRKELNEEV-KAQNIKLSVNDFIIKASALACLKVP-------EC 492
Cdd:PRK11857 80 KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVlKTEGVKLTFLPFIAKAILIALKEFPifaakydEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 493 NSSwmdtvIRQNHVVDVSVAVSTASGLITPIVFNAHIKGLTAISSDVAALAAKAREGKLQPHEFQGGTFTISNLG----M 568
Cdd:PRK11857 160 TSE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGsvgsL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961897783 569 FGVknfsAIINPPQACILAVGGSEKRlmpADNEKGFDVSS-VMSVTLSCDHRVVDGAVGAQWLAEFRKLLEKP 640
Cdd:PRK11857 235 YGV----PVINYPELAIAGVGAIIDK---AIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
216-645 |
5.40e-30 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 123.71 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 216 LPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGtrdvplgaplciivekesdiga 295
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG---------------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 296 fkDYVETGVGDVSMPPPAPAPTPVT-LQAPVPSAAPAAAAAPATPRKGRVFASPLAKKLAAekgidlaqvSGSGPDGRIT 374
Cdd:PLN02226 154 --DTVEPGTKVAIISKSEDAASQVTpSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPKA---------PSSPPPPKQS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 375 RKdiESFVPPKVAPSAaaapspaaaraapaaaaaapaapagtftdIPISNIRKVIAQRLMQSKQTIPHYYLSVDVNMDQV 454
Cdd:PLN02226 223 AK--EPQLPPKERERR-----------------------------VPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 455 LELRKELNEE-VKAQNIKLSVNDFIIKASALACLKVPECNSSW-MDTVIRQNHVvDVSVAVSTASGLITPIVFNAHIKGL 532
Cdd:PLN02226 272 MKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 533 TAISSDVAALAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGGSEKRLMPAdnekGFDV--SSVM 610
Cdd:PLN02226 351 AEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVV----GGSVvpRPMM 426
|
410 420 430
....*....|....*....|....*....|....*
gi 961897783 611 SVTLSCDHRVVDGAVGAQWLAEFRKLLEKPVTMLL 645
Cdd:PLN02226 427 YVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
86-157 |
8.10e-26 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 111.16 E-value: 8.10e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRDVNVGSVICI 157
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAV 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
84-157 |
9.77e-24 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 94.78 E-value: 9.77e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961897783 84 QKVELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRdVNVGSVICI 157
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
214-295 |
1.03e-23 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 104.61 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 214 IALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRDVPLGAPLCIIV---EKE 290
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLeegESA 84
|
....*
gi 961897783 291 SDIGA 295
Cdd:PRK11892 85 SDAGA 89
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
212-286 |
2.17e-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: 94.01 E-value: 2.17e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961897783 212 MKIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCII 286
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
214-286 |
1.38e-21 |
|
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: 88.65 E-value: 1.38e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961897783 214 IALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCII 286
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
86-157 |
2.05e-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: 82.81 E-value: 2.05e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTrDVNVGSVICI 157
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
214-287 |
4.17e-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: 81.65 E-value: 4.17e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961897783 214 IALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTrDVPLGAPLCIIV 287
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
344-379 |
8.01e-17 |
|
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: 74.26 E-value: 8.01e-17
10 20 30
....*....|....*....|....*....|....*.
gi 961897783 344 VFASPLAKKLAAEKGIDLAQVSGSGPDGRITRKDIE 379
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
86-147 |
5.29e-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: 70.16 E-value: 5.29e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTR 147
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
213-296 |
4.51e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 71.13 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 213 KIALPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTrDVPLGAPLCIIVEKE-- 290
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEvs 82
|
....*..
gi 961897783 291 -SDIGAF 296
Cdd:PRK14875 83 dAEIDAF 89
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
84-160 |
6.55e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 67.66 E-value: 6.55e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961897783 84 QKVELPALSPTMQTGTIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTrDVNVGSVICITVD 160
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVAD 78
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
214-286 |
3.75e-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: 56.45 E-value: 3.75e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961897783 214 IALPALSPTMTMGTVQrWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCII 286
Cdd:pfam00364 3 IKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
86-157 |
5.77e-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: 55.68 E-value: 5.77e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961897783 86 VELPALSPTMQTGtIARWEKKEGDKISEGDLIAEVETDKATVGFEMLEECYLAKILVPEGTRdVNVGSVICI 157
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
542-637 |
3.94e-08 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 56.82 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961897783 542 LAAKAREGKLQPHEFQGGTFTISNLGMFGVKNFSAIINPPQACILAVGG----------SEKRLmpadNEKGfdVSSVMS 611
Cdd:PRK12270 249 IVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefqgaSEERL----AELG--ISKVMT 322
|
90 100
....*....|....*....|....*.
gi 961897783 612 VTLSCDHRVVDGAVGAQWLAEFRKLL 637
Cdd:PRK12270 323 LTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
226-286 |
3.08e-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: 36.63 E-value: 3.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961897783 226 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILISEGTRdVPLGAPLCII 286
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
|
|
| |
