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Conserved domains on  [gi|1716962985|ref|NP_001358965|]
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dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial isoform 7 [Homo sapiens]

Protein Classification

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase( domain architecture ID 11492247)

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (E2) ; the pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle

CATH:  2.40.50.100
EC:  2.3.1.12
Gene Ontology:  GO:0045254|GO:0016746

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 179-605 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: 656.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 179 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 258
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 259 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 334
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 335 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 411
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 412 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 491
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 492 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 570
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716962985 571 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PRK11892 super family cl36077
pyruvate dehydrogenase subunit beta; Provisional
 80-133 1.98e-10

pyruvate dehydrogenase subunit beta; Provisional


The actual alignment was detected with superfamily member PRK11892:

Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 63.40  E-value: 1.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962985  80 GDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 133
Cdd:PRK11892   33 GDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 179-605 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: 656.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 179 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 258
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 259 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 334
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 335 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 411
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 412 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 491
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 492 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 570
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716962985 571 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 170-605 2.57e-172

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 500.54  E-value: 2.57e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 170 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 249
Cdd:PLN02744  106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 250 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 329
Cdd:PLN02744  186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 330 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSID 409
Cdd:PLN02744  266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 410 VNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 487
Cdd:PLN02744  341 TRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 488 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 566
Cdd:PLN02744  421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1716962985 567 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PLN02744  501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 394-604 1.28e-93

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 286.36  E-value: 1.28e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 394 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 470
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 471 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 550
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962985 551 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 604
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 177-251 1.22e-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: 97.48  E-value: 1.22e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716962985 177 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 251
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 178-252 3.38e-20

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 84.73  E-value: 3.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716962985 178 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 252
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 80-133 1.98e-10

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 63.40  E-value: 1.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962985  80 GDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 133
Cdd:PRK11892   33 GDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 78-123 5.75e-10

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: 55.49  E-value: 5.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1716962985  78 SEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 123
Cdd:cd06849    29 EEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 78-123 3.64e-08

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: 50.84  E-value: 3.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1716962985  78 SEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICI 123
Cdd:COG0508    31 KEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 179-605 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: 656.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 179 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 258
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 259 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 334
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 335 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 411
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 412 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 491
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 492 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 570
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716962985 571 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 170-605 2.57e-172

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 500.54  E-value: 2.57e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 170 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 249
Cdd:PLN02744  106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 250 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 329
Cdd:PLN02744  186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 330 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSID 409
Cdd:PLN02744  266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 410 VNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 487
Cdd:PLN02744  341 TRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 488 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 566
Cdd:PLN02744  421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1716962985 567 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PLN02744  501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 178-605 4.69e-150

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 438.46  E-value: 4.69e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 178 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEAD 257
Cdd:PRK11856    4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 258 ISAFADYRPTEVTDLKPQVPPPtpppvaavpptpqPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTG 337
Cdd:PRK11856   83 EAAAAAEAAPEAPAPEPAPAAA-------------AAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 338 PDGRITKKDIDSFVPSKVAPAPAAVVPPTGPgmAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLL 417
Cdd:PRK11856  150 PGGRITKEDVEAAAAAAAPAAAAAAAAAAAP--PAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 418 VRKELNKILEgrsKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAN 497
Cdd:PRK11856  228 LRKQLKAIGV---KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 498 DVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCD 577
Cdd:PRK11856  305 EIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMPLSLSFD 382

                         410       420
                  ....*....|....*....|....*...
gi 1716962985 578 HRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PRK11856  383 HRVIDGADAARFLKALKELLENPALLLL 410
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 394-604 1.28e-93

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 286.36  E-value: 1.28e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 394 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 470
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 471 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 550
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962985 551 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 604
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 78-605 2.74e-85

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 276.32  E-value: 2.74e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985  78 SEGDLI------AEVETDKATVGFESLEECYMAKILVAEGTRdVPIGA-IICITVGKPEDIEAfknytlDSSAAPTPQAA 150
Cdd:PRK11855   24 KEGDTVeedqplVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGlLAVIEAAGAAAAAA------APAAAAAPAAA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 151 PAPTPAATASPPTPSAQAPGSSYpphMQVLLPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEG 228
Cdd:PRK11855   97 AAAAPAPAAAAPAAAAAAAGGGV---VEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATM--EIpsPVAG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 229 YLAKILVPEGTRdVPLGTPLcIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVaavpptpqplAPTPSAPCPATPAG 308
Cdd:PRK11855  171 VVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAA----------AAAPAAAAPAAAAA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 309 PKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV-----PSKVAPAPAAVVPPTGPGMAPVPTGVFTD--- 380
Cdd:PRK11855  239 PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVkgamsAAAAAAAAAAAAGGGGLGLLPWPKVDFSKfge 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 381 ---IPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSW 456
Cdd:PRK11855  319 ietKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGvKLTMLPFFIKAVVAALKEFPVFNASL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 457 MDT---VIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKN 533
Cdd:PRK11855  399 DEDgdeLTYKKYF-NIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTA 477

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962985 534 FSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PRK11855  478 FTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 179-605 9.40e-76

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: 246.95  E-value: 9.40e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 179 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEkeadi 258
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 259 SAFADYRPTEVTDLKPqvppptpppvaavpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGP 338
Cdd:TIGR01347  77 GNDATAAPPAKSGEEK--------------------EETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 339 DGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPvpTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLV 418
Cdd:TIGR01347 137 TGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAA--TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMEL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 419 RKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSwmdtvIRQNHVV-----DVSVAVSTPAGLITPIVFNAHIKG 491
Cdd:TIGR01347 215 RKRYKEEFEKKHgvKLGFMSFFVKAVVAALKRFPEVNAE-----IDGDDIVykdyyDISVAVSTDRGLVVPVVRNADRMS 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 492 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVpADNEKgFDVASMMS 571
Cdd:TIGR01347 290 FADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIRPMMY 367

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1716962985 572 VTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:TIGR01347 368 LALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
179-605 1.68e-67

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 225.10  E-value: 1.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 179 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTrDVPLGTPLCIIVEKEA 256
Cdd:PRK05704    5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 257 DISAFADYRPTEvtdlkpqvppptpppvaavpptPQPLAPTPSAPCPATPAGPKGrvfVSPLAKKLAVEKGIDLTQVKGT 336
Cdd:PRK05704   82 AGAAAAAAAAAA----------------------AAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVKGT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 337 GPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIphyylSI-----DVN 411
Cdd:PRK05704  137 GKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTT-----AMlttfnEVD 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 412 MGEVLLVRKELNKILEGR--SKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHI 489
Cdd:PRK05704  212 MTPVMDLRKQYKDAFEKKhgVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQ 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 490 KGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASM 569
Cdd:PRK05704  292 LSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPM 369

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1716962985 570 MSVTLSCDHRVVDG--AVGaqWLAEFRKYLEKPITMLL 605
Cdd:PRK05704  370 MYLALSYDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 181-605 1.76e-62

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 212.24  E-value: 1.76e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 181 LPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIvekeaDISA 260
Cdd:PTZ00144   49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEI-----DTGG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 261 FADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPkgrvfvSPLAKKLAvekgidlTQVKGTGPDG 340
Cdd:PTZ00144  123 APPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEP------APAAKPPP-------TPVARADPRE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 341 ritkkdidsfvpskvapapaavvpptgpgmapvptgvfTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRK 420
Cdd:PTZ00144  190 --------------------------------------TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 421 ELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAND 498
Cdd:PTZ00144  232 EYKDDFQKKHgvKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 499 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCDH 578
Cdd:PTZ00144  312 LADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYLALTYDH 389

                         410       420
                  ....*....|....*....|....*..
gi 1716962985 579 RVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PTZ00144  390 RLIDGRDAVTFLKKIKDLIEDPARMLL 416
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 191-605 4.61e-61

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 213.71  E-value: 4.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 191 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTpLCIIVEKEADISAFAdyrPTEVT 270
Cdd:PRK11854  219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAA---PAKQE 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 271 DLKPQVPPPTPPPVAAvpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSF 350
Cdd:PRK11854  294 AAAPAPAAAKAEAPAA--------APAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 351 V----PSKVAPAPAAVVPPTGPGMAPVPT------GVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRK 420
Cdd:PRK11854  366 VkdavKRAEAAPAAAAAGGGGPGLLPWPKvdfskfGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRK 445

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 421 ELNKILEGRS---KISVNDFIIKASALACLKVPEANSSWMD---TVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVET 494
Cdd:PRK11854  446 QQNAEAEKRKlgvKITPLVFIMKAVAAALEQMPRFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVFKDVNKKGIIE 524

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 495 IANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTL 574
Cdd:PRK11854  525 LSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAME--PVWNGKEFAPRLMLPLSL 602

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1716962985 575 SCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PRK11854  603 SYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 313-605 9.83e-58

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 197.44  E-value: 9.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 313 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP-SKVAPAPAAVVPPTGPGMAP---VPTGVFTDIPISNIRR 388
Cdd:PRK14843   49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPeNIENDSIKSPAQIEKVEEVPdnvTPYGEIERIPMTPMRK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 389 VIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGR-SKISVNDFIIKASALACLKVPEANSSWMD---TVIRQ 463
Cdd:PRK14843  129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATgKKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 464 NHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQA 543
Cdd:PRK14843  209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962985 544 CILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PRK14843  288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 167-598 1.17e-57

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: 203.32  E-value: 1.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 167 QAPGSSYPPH------MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEgTR 240
Cdd:TIGR02927 111 EAPAPAAPQAggsgeaTEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DD 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 241 DVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPK----GRVFVS 316
Cdd:TIGR02927 190 TVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVssgdSGPYVT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 317 PLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSfvPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIP-------------I 383
Cdd:TIGR02927 270 PLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLA--AAKAAEEARAAAAAPAAAAAPAAPAAAAKPAepdtaklrgttqkM 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 384 SNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTV- 460
Cdd:TIGR02927 348 NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNgvNLTFLPFFVQAVTEALKAHPNVNASYNAETk 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 461 -IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIIN 539
Cdd:TIGR02927 428 eVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILN 507

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962985 540 PPQACILAIGASEDKLVPADNEKGFDVASMMSVT---LSCDHRVVDGAVGAQWLAEFRKYLE 598
Cdd:TIGR02927 508 PPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLVDGADAGRFLTTIKKRLE 569
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 199-605 1.75e-57

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: 202.41  E-value: 1.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 199 KVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPp 278
Cdd:TIGR01348 138 KVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAAT- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 279 ptpppvaavpptpQPLAPTPSAPCPATPAGPKGR--------VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSF 350
Cdd:TIGR01348 216 -------------QPEPAAAPAAAKAQAPAPQQAgtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRF 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 351 V--PSKVAPAPAAVVPPTGPGMAPVPTGVFT------DIPISNIRRVIAQRLMQSKQTIPH--YYLSIDVNMGEVLLVRK 420
Cdd:TIGR01348 283 VkePSVRAQAAAASAAGGAPGALPWPNVDFSkfgeveEVDMSRIRKISGANLTRNWTMIPHvtHFDKADITEMEAFRKQQ 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 421 ELNKILEGrSKISVNDFIIKASALACLKVPEANSSWM---DTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIAN 497
Cdd:TIGR01348 363 NAAVEKEG-VKLTVLHILMKAVAAALKKFPKFNASLDlggEQLILKKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELAL 440

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 498 DVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILaiGASEDKLVPADNEKGFDVASMMSVTLSCD 577
Cdd:TIGR01348 441 ELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKEFEPRLMLPLSLSYD 518

                         410       420
                  ....*....|....*....|....*...
gi 1716962985 578 HRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:TIGR01348 519 HRVIDGADAARFTTYICESLADIRRLLL 546
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 195-605 8.71e-51

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 180.69  E-value: 8.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 195 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGtrD-VPLGTPLC-IIVEKEADISAFADYRPTEVTDL 272
Cdd:PLN02528   17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DiVKVGETLLkIMVEDSQHLRSDSLLLPTDSSNI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 273 KpqvppptpppvaavpptpqplaptpSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP 352
Cdd:PLN02528   95 V-------------------------SLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 353 SK-VAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA----QRLMQSKQT----IPHYYLSIDVNMGEVLLVRKELN 423
Cdd:PLN02528  150 QKgVVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPlrgfQRAMVKTMTaaakVPHFHYVEEINVDALVELKASFQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 424 KI-LEGRSKISVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAGLITPIVFNAHIKGVETIAND 498
Cdd:PLN02528  230 ENnTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEITKE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 499 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDklVPADNEKGFDV-ASMMSVTLSCD 577
Cdd:PLN02528  308 LSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIGAD 385

                         410       420
                  ....*....|....*....|....*...
gi 1716962985 578 HRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PLN02528  386 HRVLDGATVARFCNEWKSYVEKPELLML 413
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 312-600 1.78e-40

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 149.56  E-value: 1.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 312 RVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV------PSKVAPAPAAVVPPTGPGMAPVPTGVFTDI---P 382
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGkreK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 383 ISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGRS-KISVNDFIIKASALACLKVP-------EAN 453
Cdd:PRK11857   81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSvKDPVLKTEGvKLTFLPFIAKAILIALKEFPifaakydEAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 454 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKN 533
Cdd:PRK11857  161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716962985 534 FSAIINPPQACILAIGASEDKlvpADNEKGFDVAS-MMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKP 600
Cdd:PRK11857  236 GVPVINYPELAIAGVGAIIDK---AIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 178-316 3.31e-29

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 120.79  E-value: 3.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 178 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEAD 257
Cdd:PRK11892    4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1716962985 258 ISAFADyRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVS 316
Cdd:PRK11892   84 ASDAGA-APAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVT 141
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 177-605 7.82e-29

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 119.86  E-value: 7.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 177 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPlGTPLCIIVEKEA 256
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEP-GTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 257 DISAFA-DYRPTEVTDLKPQVPPPTPPPVAAVPPtpqPLAPTPSAPCPATPAgpkgrvfvsplakklavekgidltqvKG 335
Cdd:PLN02226  171 AASQVTpSQKIPETTDPKPSPPAEDKQKPKVESA---PVAEKPKAPSSPPPP--------------------------KQ 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 336 TGPDGRITKKDIDSFVPskvapapaavvpptgpgmapvptgvftdipISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEV 415
Cdd:PLN02226  222 SAKEPQLPPKERERRVP------------------------------MTRLRKRVATRLKDSQNTFALLTTFNEVDMTNL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 416 LLVRKEL-NKILEGRS-KISVNDFIIKASALACLKVPEANSSW-MDTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGV 492
Cdd:PLN02226  272 MKLRSQYkDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNF 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 493 ETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAsedkLVPADNEKGFDVA--SMM 570
Cdd:PLN02226  351 AEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHS----IVSRPMVVGGSVVprPMM 426

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716962985 571 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 605
Cdd:PLN02226  427 YVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 177-251 1.22e-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: 97.48  E-value: 1.22e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716962985 177 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 251
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 178-251 5.89e-24

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: 95.59  E-value: 5.89e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716962985 178 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 251
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 178-252 3.38e-20

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 84.73  E-value: 3.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716962985 178 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 252
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 313-348 6.11e-15

e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.


Pssm-ID: 460710 [Multi-domain]  Cd Length: 36  Bit Score: 68.48  E-value: 6.11e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1716962985 313 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDID 348
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 179-263 2.21e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.90  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985 179 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEKE--- 255
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEvsd 83


                  ....*...
gi 1716962985 256 ADISAFAD 263
Cdd:PRK14875   84 AEIDAFIA 91
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 178-251 9.92e-12

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 60.69  E-value: 9.92e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716962985 178 QVLLPALSPTMTMGTVQrWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 251
Cdd:pfam00364   2 EIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 80-133 1.98e-10

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 63.40  E-value: 1.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962985  80 GDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 133
Cdd:PRK11892   33 GDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 78-123 5.75e-10

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: 55.49  E-value: 5.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1716962985  78 SEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 123
Cdd:cd06849    29 EEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 78-123 3.64e-08

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: 50.84  E-value: 3.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1716962985  78 SEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICI 123
Cdd:COG0508    31 KEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 487-597 1.31e-06

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 51.81  E-value: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985  487 AHIKGVETIA--------NDVVSlatKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA-------- 550
Cdd:PRK12270   229 PAIKGAETMDfaqfwaayEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefq 305

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1716962985  551 --SEDKLvpadNEKGfdVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYL 597
Cdd:PRK12270   306 gaSEERL----AELG--ISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 78-134 4.84e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.09  E-value: 4.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962985  78 SEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICITV---GKPEDIEAF 134
Cdd:PRK14875   31 EKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVAdaeVSDAEIDAF 89
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 78-123 2.28e-04

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: 39.73  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1716962985  78 SEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 123
Cdd:cd06663    28 KKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVK 72
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 191-251 1.05e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 37.78  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1716962985 191 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 251
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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