|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
138-565 |
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: 597.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 138 ITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 217
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 218 P-AFADY--QAAAVTDMKAPAPPPPPPQvmaTPAAAPPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLT 294
Cdd:TIGR01349 82 AdAFKNYklESSASPAPKPSEIAPTAPP---SAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 295 QVKGTGPDGRITKKDVESFVPSKAAPAAAPEAVPGVAAAPE------GTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSI 368
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAaapvstGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 369 DVNMGKVLVLRKELNQEVSENIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAH 448
Cdd:TIGR01349 239 ECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 449 IKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKE-ILVPADNEKGFDVA 527
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDvAVVDNDEEKGFAVA 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 930241179 528 SVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:TIGR01349 399 SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
129-565 |
2.04e-165 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 481.28 E-value: 2.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 129 GSSYPPHMQITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 208
Cdd:PLN02744 106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 209 IIVEKEADIPAFADYQAAAVTDMKAPAPPPPPPQVMatpaAAPPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAE 288
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPK----EEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAED 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 289 KGIDLTQVKGTGPDGRITKKDVESFVPSKAAPAAAPEAVpgVAAAPEGTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSI 368
Cdd:PLN02744 262 NNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPST--DSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 369 DVNMGKVLVLRKELN--QEVSENIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFN 446
Cdd:PLN02744 340 DTRVDKLMALRSQLNslQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 447 AHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNL-GMYGIKNFSAIINPPQACILAVGSSKEILVPADNEKGFD 525
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYN 499
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 930241179 526 VASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PLN02744 500 FASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
354-564 |
5.36e-91 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 278.27 E-value: 5.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 354 LMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEVS-ENIKLSVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 430
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAAdEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 431 VAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGS 510
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 930241179 511 SKEilVPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTML 564
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
10-91 |
4.96e-25 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 108.08 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 10 VALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRDVPIGAIICITVEKPEHI 89
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESA 84
|
..
gi 930241179 90 DA 91
Cdd:PRK11892 85 SD 86
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
136-210 |
3.62e-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: 95.93 E-value: 3.62e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930241179 136 MQITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 210
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
8-81 |
6.21e-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: 92.47 E-value: 6.21e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930241179 8 QKVALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIICI 81
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
137-211 |
1.20e-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: 83.19 E-value: 1.20e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930241179 137 QITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 211
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
12-81 |
3.76e-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: 3.76e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 12 LPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTrDVPIGAIICI 81
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
10-81 |
1.42e-09 |
|
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: 54.53 E-value: 1.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930241179 10 VALPALSPTMQMGtIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIICI 81
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 ... |
138-565 |
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: 597.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 138 ITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 217
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 218 P-AFADY--QAAAVTDMKAPAPPPPPPQvmaTPAAAPPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLT 294
Cdd:TIGR01349 82 AdAFKNYklESSASPAPKPSEIAPTAPP---SAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 295 QVKGTGPDGRITKKDVESFVPSKAAPAAAPEAVPGVAAAPE------GTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSI 368
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAaapvstGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 369 DVNMGKVLVLRKELNQEVSENIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAH 448
Cdd:TIGR01349 239 ECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 449 IKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKE-ILVPADNEKGFDVA 527
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDvAVVDNDEEKGFAVA 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 930241179 528 SVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:TIGR01349 399 SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
129-565 |
2.04e-165 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 481.28 E-value: 2.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 129 GSSYPPHMQITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 208
Cdd:PLN02744 106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 209 IIVEKEADIPAFADYQAAAVTDMKAPAPPPPPPQVMatpaAAPPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAE 288
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPK----EEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAED 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 289 KGIDLTQVKGTGPDGRITKKDVESFVPSKAAPAAAPEAVpgVAAAPEGTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSI 368
Cdd:PLN02744 262 NNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPST--DSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 369 DVNMGKVLVLRKELN--QEVSENIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFN 446
Cdd:PLN02744 340 DTRVDKLMALRSQLNslQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 447 AHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNL-GMYGIKNFSAIINPPQACILAVGSSKEILVPADNEKGFD 525
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYN 499
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 930241179 526 VASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PLN02744 500 FASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
137-565 |
6.57e-150 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 436.91 E-value: 6.57e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 137 QITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEAD 216
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 217 IPAFADYQAAAVTdmkapappppppqvmatPAAAPPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLTQV 296
Cdd:PRK11856 83 EAAAAAEAAPEAP-----------------APEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 297 KGTGPDGRITKKDVESFV-PSKAAPAAAPEAVPGVAAAPEGTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKV 375
Cdd:PRK11856 146 KGSGPGGRITKEDVEAAAaAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 376 LVLRKELNQEvseNIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLAAI 455
Cdd:PRK11856 226 LALRKQLKAI---GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 456 SKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKEILVPADNEkgFDVASVMSVTLS 535
Cdd:PRK11856 303 AREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMPLSLS 380
|
410 420 430
....*....|....*....|....*....|
gi 930241179 536 CDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PRK11856 381 FDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
354-564 |
5.36e-91 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 278.27 E-value: 5.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 354 LMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEVS-ENIKLSVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 430
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAAdEETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 431 VAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGS 510
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 930241179 511 SKEilVPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTML 564
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
22-565 |
2.65e-88 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 282.87 E-value: 2.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 22 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIIcITVEKPEHIDAfknytldsAA 101
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGLL-AVIEAAGAAAA--------AA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 102 AAAPAASVPPPPAAAPSPPPQPSPQAPGSSYPPHMQITLPALSpTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIgf 181
Cdd:PRK11855 86 APAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATM-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 182 EV--QEEGYLAKILVPEGTRdVPLGTPLcIIVEKEADIPAFADYQAAAVTDMKAPAPPPPPPQvmatpaaapppaqpAAA 259
Cdd:PRK11855 163 EIpsPVAGVVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPA--------------AAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 260 PAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVESFVPSKAAPAAAPEAVPGVAAAPE---- 335
Cdd:PRK11855 227 APAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGlgll 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 336 ----------GTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEVS-ENIKLSVNDFIIKASAL 404
Cdd:PRK11855 307 pwpkvdfskfGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEkAGVKLTMLPFFIKAVVA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 405 ACLKVPEANSSWMDT---VIRQNHvVDVSVAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTF 481
Cdd:PRK11855 387 ALKEFPVFNASLDEDgdeLTYKKY-FNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 482 TISNLGMYGIKNFSAIINPPQACILAVGSSkEILvPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPV 561
Cdd:PRK11855 466 TISSLGGIGGTAFTPIINAPEVAILGVGKS-QMK-PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPR 543
|
....
gi 930241179 562 TMLL 565
Cdd:PRK11855 544 RMLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
138-565 |
6.47e-73 |
|
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: 6.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 138 ITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIvEKEADI 217
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAIL-EEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 218 PAfadyQAAAVTDMKAPAPPPPPPQVMATPAaapppaqpaaapapaapsagpprkGGRVVISPLAKKLAAEKGIDLTQVK 297
Cdd:TIGR01347 81 TA----APPAKSGEEKEETPAASAAAAPTAA------------------------ANRPSLSPAARRLAKEHGIDLSAVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 298 GTGPDGRITKKDVESfvPSKAAPAAAPEAVPGVAAAPEG---TFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGK 374
Cdd:TIGR01347 133 GTGVTGRVTKEDIIK--KTEAPASAQPPAAAAAAAAPAAatrPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 375 VLVLRKELNQEVSE--NIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGL 452
Cdd:TIGR01347 211 VMELRKRYKEEFEKkhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 453 AAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKEILVpADNEKgFDVASVMSV 532
Cdd:TIGR01347 291 ADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIRPMMYL 368
|
410 420 430
....*....|....*....|....*....|...
gi 930241179 533 TLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:TIGR01347 369 ALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
138-565 |
4.40e-71 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 233.57 E-value: 4.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 138 ITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTrDVPLGTPLCIIVEKEA 215
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 216 DIPAFADYQAAAVTdmkapappppppqvmatpaaapppaqpaaAPAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLTQ 295
Cdd:PRK05704 82 AGAAAAAAAAAAAA-----------------------------AAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 296 VKGTGPDGRITKKDVESFVPSKAAPAAAPEAVPGVAA-APEGTFTDI--PISNIRRVIAQRLMQSKQTIPHYYLSIDVNM 372
Cdd:PRK05704 133 VKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAApAPLGARPEErvPMTRLRKTIAERLLEAQNTTAMLTTFNEVDM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 373 GKVLVLRKELnQEVSE---NIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHI 449
Cdd:PRK05704 213 TPVMDLRKQY-KDAFEkkhGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 450 KGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKEILVPADNEkgFDVASV 529
Cdd:PRK05704 292 LSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPM 369
|
410 420 430
....*....|....*....|....*....|....*.
gi 930241179 530 MSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PRK05704 370 MYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
10-558 |
8.99e-66 |
|
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: 224.51 E-value: 8.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 10 VALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEgTRDVPIGAIICITVEKPEHI 89
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPGEAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 90 DAFKNYTLDSAAAAAPAASVPPPPAAAPSPPPQPSPQAPGSSYPPhmqITLPALSPTMTMGTVQRWEKKVGEKLNEGDLL 169
Cdd:TIGR02927 84 SEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATE---VKMPELGESVTEGTVTSWLKAVGDTVEVDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 170 AEIETDKATIGFEVQEEGYLAKILVPEgTRDVPLGTPLCIIVEKEADIPAFADYQAAAVTDMKAPAPPPPPPQVMATPAA 249
Cdd:TIGR02927 161 LEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 250 APPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVESfVPSKAAPAAAPEAVPG 329
Cdd:TIGR02927 240 PPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLA-AAKAAEEARAAAAAPA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 330 VAAAPEGTF---------------TDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEVSEN--IKL 392
Cdd:TIGR02927 319 AAAAPAAPAaaakpaepdtaklrgTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKngVNL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 393 SVNDFIIKASALACLKVPEANSSWMDTV--IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGK 470
Cdd:TIGR02927 399 TFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 471 LQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGS---SKEILVPADNEKGFDVASVMSVTLSCDHRVVDGAVGA 547
Cdd:TIGR02927 479 LKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAivkRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAG 558
|
570
....*....|.
gi 930241179 548 QWLAEFKNFLE 558
Cdd:TIGR02927 559 RFLTTIKKRLE 569
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
138-565 |
2.51e-62 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 211.08 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 138 ITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEKEADI 217
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEIDTGGAPP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 218 PAFADYQAAAVTDMKApappppppqvmatpaaapppaqpaaapapaapsagpprkggrvvisPLAKKLAAEKgidltqvk 297
Cdd:PTZ00144 126 AAAPAAAAAAKAEKTT----------------------------------------------PEKPKAAAPT-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 298 gtgPDGRITKKDVESFVPSKAAPAAAPEAVPGVAAAPEGTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKVLV 377
Cdd:PTZ00144 152 ---PEPPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALME 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 378 LRKELNQEVSE--NIKLSVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLAAI 455
Cdd:PTZ00144 229 LRKEYKDDFQKkhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 456 SKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKEILVPADNEkgFDVASVMSVTLS 535
Cdd:PTZ00144 309 EKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYLALT 386
|
410 420 430
....*....|....*....|....*....|
gi 930241179 536 CDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PTZ00144 387 YDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
276-565 |
1.98e-58 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 198.59 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 276 VVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVESFVPS-------KAAPAAAPEAVPGVAAAPEGTFTDIPISNIRR 348
Cdd:PRK14843 49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPEniendsiKSPAQIEKVEEVPDNVTPYGEIERIPMTPMRK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 349 VIAQRLMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEVSENI--KLSVNDFIIKASALACLKVPEANSSWMD---TVIRQ 423
Cdd:PRK14843 129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATgkKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 424 NHVvDVSVAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQA 503
Cdd:PRK14843 209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930241179 504 CILAVGSSKEILVPADNEkgFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PRK14843 288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
30-565 |
2.45e-54 |
|
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: 192.78 E-value: 2.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 30 KEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIICItvekpehIDAFKNYTLDSAAAAAPAASV 109
Cdd:TIGR01348 22 KPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDT-LPVGGVIAT-------LEVGAGAQAQAEAKKEAAPAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 110 PPPPAAAPSPPPQPSPQAPGSSYpphMQITLPALSpTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYL 189
Cdd:TIGR01348 94 TAGAPAPAAQAQAAPAAGQSSGV---QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 190 AKILVPEGTRdVPLGTpLCIIVEKEADIPAFADYQAAAvtdmkapappPPPPQVMATPAAAPPPAQPAAAPAPAAPSAGP 269
Cdd:TIGR01348 170 KSVKVKVGDS-VPTGD-LILTLSVAGSTPATAPAPASA----------QPAAQSPAATQPEPAAAPAAAKAQAPAPQQAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 270 PRKGGRVV-ISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVESFV--PSKAAPAAAPEAVPGVAAAPE---------GT 337
Cdd:TIGR01348 238 TQNPAKVDhAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVkePSVRAQAAAASAAGGAPGALPwpnvdfskfGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 338 FTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEVS-ENIKLSVNDFIIKASALACLKVPEANSSW 416
Cdd:TIGR01348 318 VEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEkEGVKLTVLHILMKAVAAALKKFPKFNASL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 417 M---DTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKN 493
Cdd:TIGR01348 398 DlggEQLILKKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTA 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930241179 494 FSAIINPPQACILAVgsSKEILVPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:TIGR01348 477 FTPIVNAPEVAILGV--SKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
150-565 |
7.15e-54 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 193.30 E-value: 7.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 150 GTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTpLCIIVEKEADIPAFADYQAAAVT 229
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAAPAKQEAAA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 230 DmkapappppppqvmaTPAAAPPPAQPAAAPAPAAPSAGPPRKGGRVVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKD 309
Cdd:PRK11854 297 P---------------APAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 310 VESFVpskaaPAAAPEAVPGVAAAPEGT---------------FTDI---PISNIRRVIAQRLMQSKQTIPHYYLSIDVN 371
Cdd:PRK11854 362 VQAYV-----KDAVKRAEAAPAAAAAGGggpgllpwpkvdfskFGEIeevELGRIQKISGANLHRNWVMIPHVTQFDKAD 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 372 MGKVLVLRKELNQEvSENIKLSVN----DFIIKASALACLKVPEANSSWMD---TVIRQNHVvDVSVAVSTPAGLITPIV 444
Cdd:PRK11854 437 ITELEAFRKQQNAE-AEKRKLGVKitplVFIMKAVAAALEQMPRFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVF 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 445 FNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILavGSSKEILVPADNEKGF 524
Cdd:PRK11854 515 KDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAIL--GVSKSAMEPVWNGKEF 592
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 930241179 525 DVASVMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PRK11854 593 APRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
154-565 |
1.38e-52 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 184.92 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 154 RWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLC-IIVEKEADIPAFADYQAAAVTDMK 232
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETLLkIMVEDSQHLRSDSLLLPTDSSNIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 233 APAPPPPPPQVMatpaaapppaqpaaapapaapsagpprkgGRVVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVES 312
Cdd:PLN02528 96 SLAESDERGSNL-----------------------------SGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 313 FVPSKAAPAAAPEAVPGVAAAPEGTFTDIPI----SNIRRVIA----QRLMQSKQT----IPHYYLSIDVNMGKVLVLRK 380
Cdd:PLN02528 147 YAAQKGVVKDSSSAEEATIAEQEEFSTSVSTpteqSYEDKTIPlrgfQRAMVKTMTaaakVPHFHYVEEINVDALVELKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 381 ELNQEVSEN-IKLSVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAGLITPIVFNAHIKGLAAI 455
Cdd:PLN02528 227 SFQENNTDPtVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 456 SKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGSSKEilVPADNEKGFDV-ASVMSVTL 534
Cdd:PLN02528 305 TKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTI 382
|
410 420 430
....*....|....*....|....*....|.
gi 930241179 535 SCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PLN02528 383 GADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
275-560 |
3.97e-43 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 156.11 E-value: 3.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 275 RVVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVESFV---PSKAAPAAAPEAVPGVAAAPEGTFTDIP--------- 342
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslKSAPTPAEAASVSSAQQAAKTAAPAAAPpklegkrek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 343 ISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKVLVLRKELNQEV--SENIKLSVNDFIIKASALACLKVP-------EAN 413
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVlkTEGVKLTFLPFIAKAILIALKEFPifaakydEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 414 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLAAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKN 493
Cdd:PRK11857 161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930241179 494 FSAIINPPQACILAVGSskeILVPADNEKGFDVAS-VMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKP 560
Cdd:PRK11857 236 GVPVINYPELAIAGVGA---IIDKAIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
136-565 |
5.25e-30 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 122.94 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 136 MQITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPlGTPLCIIVEKEA 215
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEP-GTKVAIISKSED 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 216 DIPAFADYQAAAVTdmkapappppppqvmatpaaapppaqpaaaPAPAAPSAGPPRKGGRVVISPLAKKLAAekgidltq 295
Cdd:PLN02226 171 AASQVTPSQKIPET------------------------------TDPKPSPPAEDKQKPKVESAPVAEKPKA-------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 296 vKGTGPDGRITKKdvESFVPskaapaaapeavpgvaaaPEGTFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGKV 375
Cdd:PLN02226 213 -PSSPPPPKQSAK--EPQLP------------------PKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 376 LVLRKELNQEVSEN--IKLSVNDFIIKASALACLKVPEANSSW-MDTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGL 452
Cdd:PLN02226 272 MKLRSQYKDAFYEKhgVKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 453 AAISKDVASLAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGS--SKEILVpadnekGFDVA--S 528
Cdd:PLN02226 351 AEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSivSRPMVV------GGSVVprP 424
|
410 420 430
....*....|....*....|....*....|....*..
gi 930241179 529 VMSVTLSCDHRVVDGAVGAQWLAEFKNFLEKPVTMLL 565
Cdd:PLN02226 425 MMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
137-227 |
4.06e-26 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 111.55 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 137 QITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEAD 216
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83
|
90
....*....|.
gi 930241179 217 IPAFADYQAAA 227
Cdd:PRK11892 84 ASDAGAAPAAA 94
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
10-91 |
4.96e-25 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 108.08 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 10 VALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRDVPIGAIICITVEKPEHI 89
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESA 84
|
..
gi 930241179 90 DA 91
Cdd:PRK11892 85 SD 86
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
136-210 |
3.62e-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: 95.93 E-value: 3.62e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930241179 136 MQITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 210
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
8-81 |
6.21e-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: 92.47 E-value: 6.21e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930241179 8 QKVALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIICI 81
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
137-210 |
9.20e-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: 92.12 E-value: 9.20e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930241179 137 QITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 210
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
137-211 |
1.20e-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: 83.19 E-value: 1.20e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930241179 137 QITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 211
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
12-81 |
3.76e-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: 3.76e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 12 LPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTrDVPIGAIICI 81
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
276-311 |
1.14e-16 |
|
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: 73.49 E-value: 1.14e-16
10 20 30
....*....|....*....|....*....|....*.
gi 930241179 276 VVISPLAKKLAAEKGIDLTQVKGTGPDGRITKKDVE 311
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
10-81 |
8.78e-16 |
|
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: 72.09 E-value: 8.78e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930241179 10 VALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIICI 81
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVK 72
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
138-230 |
5.08e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.82 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 138 ITLPALSPTMTMGTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEKE--- 214
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEvsd 83
|
90
....*....|....*..
gi 930241179 215 ADIPAFAD-YQAAAVTD 230
Cdd:PRK14875 84 AEIDAFIApFARRFAPE 100
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-92 |
7.03e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.44 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 8 QKVALPALSPTMQMGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTrDVPIGAIICITVEK-- 85
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAev 81
|
....*...
gi 930241179 86 -PEHIDAF 92
Cdd:PRK14875 82 sDAEIDAF 89
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
137-210 |
1.16e-11 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 60.31 E-value: 1.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930241179 137 QITLPALSPTMTMGTVQrWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 210
Cdd:pfam00364 2 EIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
10-81 |
1.42e-09 |
|
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: 54.53 E-value: 1.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930241179 10 VALPALSPTMQMGtIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYLAKILVPEGTRdVPIGAIICI 81
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
462-544 |
1.92e-06 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 51.04 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930241179 462 LAARAREGKLQPHEFQGGTFTISNLGMYGIKNFSAIINPPQACILAVGS----------SKEILvpadNEKGfdVASVMS 531
Cdd:PRK12270 249 IVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefqgaSEERL----AELG--ISKVMT 322
|
90
....*....|...
gi 930241179 532 VTLSCDHRVVDGA 544
Cdd:PRK12270 323 LTSTYDHRIIQGA 335
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
150-210 |
2.96e-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: 36.24 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930241179 150 GTVQRWEKKVGEKLNEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 210
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
|
|
| |
