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Conserved domains on  [gi|167887549|gb|ACA05975|]
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dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex mitochondrial precursor [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 ...
 221-647 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: 657.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 300
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  301 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 376
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  377 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 453
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  454 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 533
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  534 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 612
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 167887549  613 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PRK11892 super family cl36077
pyruvate dehydrogenase subunit beta; Provisional
 96-175 4.53e-24

pyruvate dehydrogenase subunit beta; Provisional


The actual alignment was detected with superfamily member PRK11892:

Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.77  E-value: 4.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  96 LPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 175
Cdd:PRK11892   7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 221-647 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: 657.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 300
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  301 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 376
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  377 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 453
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  454 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 533
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  534 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 612
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 167887549  613 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 212-647 7.19e-172

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 500.92  E-value: 7.19e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 212 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 291
Cdd:PLN02744 106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 292 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 371
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 372 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSID 451
Cdd:PLN02744 266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 452 VNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 529
Cdd:PLN02744 341 TRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 530 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 608
Cdd:PLN02744 421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 167887549 609 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PLN02744 501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 436-646 1.23e-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: 287.52  E-value: 1.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  436 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 512
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  513 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 592
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887549  593 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 646
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 219-293 5.22e-25

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 98.63  E-value: 5.22e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887549 219 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 96-175 4.53e-24

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.77  E-value: 4.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  96 LPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 175
Cdd:PRK11892   7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 92-165 1.05e-23

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.78  E-value: 1.05e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887549  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 220-294 1.77e-20

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 85.89  E-value: 1.77e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887549 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 294
Cdd:COG0508    4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 94-165 8.23e-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: 83.96  E-value: 8.23e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887549  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICI 165
Cdd:COG0508    5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 94-165 8.14e-10

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


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 55.30  E-value: 8.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887549   94 VPLPSLSPTMQAGtIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
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 ...
 221-647 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: 657.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 300
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  301 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 376
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  377 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN 453
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  454 MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 533
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  534 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 612
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 167887549  613 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 212-647 7.19e-172

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 500.92  E-value: 7.19e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 212 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 291
Cdd:PLN02744 106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 292 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 371
Cdd:PLN02744 186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 372 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSID 451
Cdd:PLN02744 266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 452 VNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 529
Cdd:PLN02744 341 TRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 530 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 608
Cdd:PLN02744 421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 167887549 609 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PLN02744 501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 220-647 3.07e-150

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 440.77  E-value: 3.07e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEAD 299
Cdd:PRK11856   4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 300 ISAFADYRPTEVTDLKPQVPPPtpppvaavpptpqPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTG 379
Cdd:PRK11856  83 EAAAAAEAAPEAPAPEPAPAAA-------------AAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 380 PDGRITKKDIDSFVPSKVAPAPAAVVPPTGPgmAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLL 459
Cdd:PRK11856 150 PGGRITKEDVEAAAAAAAPAAAAAAAAAAAP--PAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 460 VRKELNKILEgrsKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAN 539
Cdd:PRK11856 228 LRKQLKAIGV---KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 540 DVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCD 619
Cdd:PRK11856 305 EIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMPLSLSFD 382

                        410       420
                 ....*....|....*....|....*...
gi 167887549 620 HRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 436-646 1.23e-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: 287.52  E-value: 1.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  436 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 512
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  513 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 592
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887549  593 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 646
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 106-647 7.24e-93

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 297.50  E-value: 7.24e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 106 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGA-IICITVGKPEDIEAfknytlDSS 184
Cdd:PRK11855  16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGlLAVIEAAGAAAAAA------APA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 185 AAPTPQAAPAPTPAATASPPTPSAQAPGSSYpphMQVLLPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgf 264
Cdd:PRK11855  89 AAAAPAAAAAAAPAPAAAAPAAAAAAAGGGV---VEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATM-- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 265 EV--QEEGYLAKILVPEGTRdVPLGTPLcIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVaavpptpqplAPTPSA 342
Cdd:PRK11855 163 EIpsPVAGVVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAA----------AAAPAA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 343 PCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV-----PSKVAPAPAAVVPPTGPGMAPVPT 417
Cdd:PRK11855 231 AAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVkgamsAAAAAAAAAAAAGGGGLGLLPWPK 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 418 GVFTD------IPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLK 490
Cdd:PRK11855 311 VDFSKfgeietKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGvKLTMLPFFIKAVVAALKE 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 491 VPEANSSWMDT---VIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISN 567
Cdd:PRK11855 391 FPVFNASLDEDgdeLTYKKYF-NIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISS 469

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 568 LGMFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PRK11855 470 LGGIGGTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 221-647 1.32e-75

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: 247.72  E-value: 1.32e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEkeadi 300
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  301 SAFADYRPTEVTDLKPqvppptpppvaavpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGP 380
Cdd:TIGR01347  77 GNDATAAPPAKSGEEK--------------------EETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  381 DGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPvpTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLV 460
Cdd:TIGR01347 137 TGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAA--TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMEL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  461 RKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSwmdtvIRQNHVV-----DVSVAVSTPAGLITPIVFNAHIKG 533
Cdd:TIGR01347 215 RKRYKEEFEKKHgvKLGFMSFFVKAVVAALKRFPEVNAE-----IDGDDIVykdyyDISVAVSTDRGLVVPVVRNADRMS 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  534 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVpADNEKgFDVASMMS 613
Cdd:TIGR01347 290 FADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIRPMMY 367

                         410       420       430
                  ....*....|....*....|....*....|....
gi 167887549  614 VTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:TIGR01347 368 LALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
221-647 1.13e-67

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 226.64  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTrDVPLGTPLCIIVEKEA 298
Cdd:PRK05704   5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 299 DISAFADYRPTEvtdlkpqvppptpppvaavpptPQPLAPTPSAPCPATPAGPKGrvfVSPLAKKLAVEKGIDLTQVKGT 378
Cdd:PRK05704  82 AGAAAAAAAAAA----------------------AAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVKGT 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 379 GPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIphyylSI-----DVN 453
Cdd:PRK05704 137 GKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTT-----AMlttfnEVD 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 454 MGEVLLVRKELNKILEGR--SKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHI 531
Cdd:PRK05704 212 MTPVMDLRKQYKDAFEKKhgVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQ 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 532 KGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASM 611
Cdd:PRK05704 292 LSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPM 369

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 167887549 612 MSVTLSCDHRVVDG--AVGaqWLAEFRKYLEKPITMLL 647
Cdd:PRK05704 370 MYLALSYDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 94-640 2.79e-65

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: 225.28  E-value: 2.79e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549   94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKIlVAEGTRDVPIGAIICItVGKPEDI 173
Cdd:TIGR02927   5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEI-RAPEDDTVEVGGVLAI-IGEPGEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  174 EAfknytldSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPH------MQVLLPALSPTMTMGTVQRWEKKVGEKLS 247
Cdd:TIGR02927  83 GS-------EPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAggsgeaTEVKMPELGESVTEGTVTSWLKAVGDTVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  248 EGDLLAEIETDKATIGFEVQEEGYLAKILVPEgTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVA 327
Cdd:TIGR02927 156 VDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  328 AVPPTPQPLAPTPSAPCPATPAGPK----GRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSfvPSKVAPAPAA 403
Cdd:TIGR02927 235 HAAPDPPAPAPAPAKTAAPAAAAPVssgdSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLA--AAKAAEEARA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  404 VVPPTGPGMAPVPTGVFTDIP-------------ISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEG 470
Cdd:TIGR02927 313 AAAAPAAAAAPAAPAAAAKPAepdtaklrgttqkMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLE 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  471 RS--KISVNDFIIKASALACLKVPEANSSWMDTV--IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLAT 546
Cdd:TIGR02927 393 KNgvNLTFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAA 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  547 KAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVT---LSCDHRVV 623
Cdd:TIGR02927 473 RARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLV 552

                         570
                  ....*....|....*..
gi 167887549  624 DGAVGAQWLAEFRKYLE 640
Cdd:TIGR02927 553 DGADAGRFLTTIKKRLE 569
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 106-647 1.08e-62

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 219.49  E-value: 1.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 106 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIIcITVGKPEDIEAfknytldssa 185
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VSTGSLI-MVFEVAGEAPA---------- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 186 aptpqaapaptPAATASPPTPSAQAPGSSyPPHMQVLLPALSptMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFE 265
Cdd:PRK11854 186 -----------AAPAAAEAAAPAAAPAAA-AGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVP 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 266 VQEEGYLAKILVPEGTRdVPLGTpLCIIVEKEADISAFAdyrPTEVTDLKPQVPPPTPPPVAAvpptpqplAPTPSAPCP 345
Cdd:PRK11854 252 APFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAA---PAKQEAAAPAPAAAKAEAPAA--------APAAKAEGK 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 346 ATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV----PSKVAPAPAAVVPPTGPGMAPVPT---- 417
Cdd:PRK11854 319 SEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVkdavKRAEAAPAAAAAGGGGPGLLPWPKvdfs 398

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 418 --GVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS---KISVNDFIIKASALACLKVP 492
Cdd:PRK11854 399 kfGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKlgvKITPLVFIMKAVAAALEQMP 478

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 493 EANSSWMD---TVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLG 569
Cdd:PRK11854 479 RFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIG 557

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887549 570 MFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PRK11854 558 GLGTTHFTPIVNAPEVAILGVSKSAME--PVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 223-647 3.51e-62

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 212.24  E-value: 3.51e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 223 LPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIvekeaDISA 302
Cdd:PTZ00144  49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEI-----DTGG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 303 FADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPkgrvfvSPLAKKLAvekgidlTQVKGTGPDG 382
Cdd:PTZ00144 123 APPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEP------APAAKPPP-------TPVARADPRE 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 383 ritkkdidsfvpskvapapaavvpptgpgmapvptgvfTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRK 462
Cdd:PTZ00144 190 --------------------------------------TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRK 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 463 ELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAND 540
Cdd:PTZ00144 232 EYKDDFQKKHgvKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 541 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCDH 620
Cdd:PTZ00144 312 LADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYLALTYDH 389

                        410       420
                 ....*....|....*....|....*..
gi 167887549 621 RVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PTZ00144 390 RLIDGRDAVTFLKKIKDLIEDPARMLL 416
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 114-647 3.00e-59

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: 207.81  E-value: 3.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  114 KEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIIC-ITVGKPEDIEAfknytldssaapTPQAA 192
Cdd:TIGR01348  22 KPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDT-LPVGGVIAtLEVGAGAQAQA------------EAKKE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  193 PAPTPAATASPPTPSAQAPGSSYPPH--MQVLLPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEG 270
Cdd:TIGR01348  89 AAPAPTAGAPAPAAQAQAAPAAGQSSgvQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  271 YLAKILVPEGTRdVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPpptpppvaavpptpQPLAPTPSAPCPATPAG 350
Cdd:TIGR01348 168 VVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAAT--------------QPEPAAAPAAAKAQAPA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  351 PKGR--------VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV--PSKVAPAPAAVVPPTGPGMAPVPTGVF 420
Cdd:TIGR01348 233 PQQAgtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVkePSVRAQAAAASAAGGAPGALPWPNVDF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  421 T------DIPISNIRRVIAQRLMQSKQTIPH--YYLSIDVNMGEVLLVRKELNKILEGrSKISVNDFIIKASALACLKVP 492
Cdd:TIGR01348 313 SkfgeveEVDMSRIRKISGANLTRNWTMIPHvtHFDKADITEMEAFRKQQNAAVEKEG-VKLTVLHILMKAVAAALKKFP 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  493 EANSSWM---DTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLG 569
Cdd:TIGR01348 392 KFNASLDlggEQLILKKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLG 470

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887549  570 MFGIKNFSAIINPPQACILaiGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:TIGR01348 471 GIGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 355-647 1.07e-57

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 198.21  E-value: 1.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 355 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP-SKVAPAPAAVVPPTGPGMAP---VPTGVFTDIPISNIRR 430
Cdd:PRK14843  49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPeNIENDSIKSPAQIEKVEEVPdnvTPYGEIERIPMTPMRK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 431 VIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGR-SKISVNDFIIKASALACLKVPEANSSWMD---TVIRQ 505
Cdd:PRK14843 129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATgKKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 506 NHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQA 585
Cdd:PRK14843 209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887549 586 CILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PRK14843 288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 237-647 8.26e-51

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 181.46  E-value: 8.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 237 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGtrD-VPLGTPLC-IIVEKEADISAFADYRPTEVTDL 314
Cdd:PLN02528  17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DiVKVGETLLkIMVEDSQHLRSDSLLLPTDSSNI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 315 KpqvppptpppvaavpptpqplaptpSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP 394
Cdd:PLN02528  95 V-------------------------SLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 395 SK-VAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA----QRLMQSKQT----IPHYYLSIDVNMGEVLLVRKELN 465
Cdd:PLN02528 150 QKgVVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPlrgfQRAMVKTMTaaakVPHFHYVEEINVDALVELKASFQ 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 466 KI-LEGRSKISVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAGLITPIVFNAHIKGVETIAND 540
Cdd:PLN02528 230 ENnTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEITKE 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 541 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDklVPADNEKGFDV-ASMMSVTLSCD 619
Cdd:PLN02528 308 LSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIGAD 385

                        410       420
                 ....*....|....*....|....*...
gi 167887549 620 HRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PLN02528 386 HRVLDGATVARFCNEWKSYVEKPELLML 413
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 354-642 2.01e-40

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 149.94  E-value: 2.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 354 RVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV------PSKVAPAPAAVVPPTGPGMAPVPTGVFTDI---P 424
Cdd:PRK11857   1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGkreK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 425 ISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGRS-KISVNDFIIKASALACLKVP-------EAN 495
Cdd:PRK11857  81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSvKDPVLKTEGvKLTFLPFIAKAILIALKEFPifaakydEAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 496 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKN 575
Cdd:PRK11857 161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887549 576 FSAIINPPQACILAIGASEDKlvpADNEKGFDVAS-MMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKP 642
Cdd:PRK11857 236 GVPVINYPELAIAGVGAIIDK---AIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 220-358 3.34e-29

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 121.18  E-value: 3.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEAD 299
Cdd:PRK11892   4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167887549 300 ISAFADyRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVS 358
Cdd:PRK11892  84 ASDAGA-APAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVT 141
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 219-647 9.33e-29

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 119.86  E-value: 9.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 219 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPlGTPLCIIVEKEA 298
Cdd:PLN02226  92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEP-GTKVAIISKSED 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 299 DISAFA-DYRPTEVTDLKPQVPPPTPPPVAAVPPtpqPLAPTPSAPCPATPAgpkgrvfvsplakklavekgidltqvKG 377
Cdd:PLN02226 171 AASQVTpSQKIPETTDPKPSPPAEDKQKPKVESA---PVAEKPKAPSSPPPP--------------------------KQ 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 378 TGPDGRITKKDIDSFVPskvapapaavvpptgpgmapvptgvftdipISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEV 457
Cdd:PLN02226 222 SAKEPQLPPKERERRVP------------------------------MTRLRKRVATRLKDSQNTFALLTTFNEVDMTNL 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 458 LLVRKEL-NKILEGRS-KISVNDFIIKASALACLKVPEANSSW-MDTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGV 534
Cdd:PLN02226 272 MKLRSQYkDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNF 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 535 ETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAsedkLVPADNEKGFDVA--SMM 612
Cdd:PLN02226 351 AEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHS----IVSRPMVVGGSVVprPMM 426

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 167887549 613 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 647
Cdd:PLN02226 427 YVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 219-293 5.22e-25

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 98.63  E-value: 5.22e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887549 219 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 220-293 3.39e-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: 96.36  E-value: 3.39e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887549 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06663    1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 96-175 4.53e-24

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.77  E-value: 4.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  96 LPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 175
Cdd:PRK11892   7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 92-165 1.05e-23

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.78  E-value: 1.05e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887549  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 220-294 1.77e-20

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 85.89  E-value: 1.77e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887549 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 294
Cdd:COG0508    4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 94-165 8.23e-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: 83.96  E-value: 8.23e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887549  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICI 165
Cdd:COG0508    5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 94-165 3.10e-15

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 70.93  E-value: 3.10e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887549  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06663    2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVK 72
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 355-390 5.75e-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: 68.87  E-value: 5.75e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 167887549  355 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDID 390
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 92-176 1.16e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 73.05  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICITV---G 168
Cdd:PRK14875   3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVAdaeV 81


                 ....*...
gi 167887549 169 KPEDIEAF 176
Cdd:PRK14875  82 SDAEIDAF 89
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 221-305 1.46e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.67  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEKE--- 297
Cdd:PRK14875   5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEvsd 83


                 ....*...
gi 167887549 298 ADISAFAD 305
Cdd:PRK14875  84 AEIDAFIA 91
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 220-293 5.37e-12

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


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 61.46  E-value: 5.37e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887549  220 QVLLPALSPTMTMGTVQrWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:pfam00364   2 EIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 94-165 8.14e-10

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


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 55.30  E-value: 8.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887549   94 VPLPSLSPTMQAGtIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 529-639 1.36e-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: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887549  529 AHIKGVETIA--------NDVVSlatKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA-------- 592
Cdd:PRK12270  229 PAIKGAETMDfaqfwaayEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefq 305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 167887549  593 --SEDKLvpadNEKGfdVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYL 639
Cdd:PRK12270  306 gaSEERL----AELG--ISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 233-293 9.02e-04

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: 38.17  E-value: 9.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887549 233 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06850    8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 105-129 6.20e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 35.92  E-value: 6.20e-03
                         10        20
                 ....*....|....*....|....*
gi 167887549 105 AGTIARWEKKEGDKINEGDLIAEVE 129
Cdd:PRK08225  46 AGTVKKINVQEGDFVNEGDVLLEIE 70
 
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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