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Conserved domains on  [gi|1716945216|ref|NP_001358964|]
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dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial isoform 6 [Homo sapiens]

Protein Classification

pyruvate dehydrogenase complex E2/E3BP family protein( domain architecture ID 1000906)

2-oxoacid dehydrogenase family protein similar to pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase-binding protein (E3BP)

CATH:  2.40.50.100
Gene Ontology:  GO:0045254

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDHac_trf_mito super family cl36877
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 221-611 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]


The actual alignment was detected with superfamily member TIGR01349:

Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 574.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 300
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 301 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 376
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 377 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRI---------------------- 431
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIiakrlleskqtiphyyvsiecn 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 432 --------------LEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 497
Cdd:TIGR01349 242 vdkllalrkelnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 498 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 576
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716945216 577 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PRK11892 super family cl36077
pyruvate dehydrogenase subunit beta; Provisional
 96-175 4.81e-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: 105.38  E-value: 4.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  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 ...
 221-611 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: 574.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 300
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 301 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 376
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 377 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRI---------------------- 431
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIiakrlleskqtiphyyvsiecn 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 432 --------------LEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 497
Cdd:TIGR01349 242 vdkllalrkelnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 498 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 576
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716945216 577 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 212-611 4.31e-146

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 433.51  E-value: 4.31e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 212 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 291
Cdd:PLN02744  106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 292 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 371
Cdd:PLN02744  186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 372 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRIL------------------- 432
Cdd:PLN02744  266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTasrllqskqtiphyyltvd 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 433 -------------------EGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 493
Cdd:PLN02744  341 trvdklmalrsqlnslqeaSGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 494 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 572
Cdd:PLN02744  421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1716945216 573 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PLN02744  501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 419-610 2.12e-79

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: 249.77  E-value: 2.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 419 VFTDIPISNIRRILEG--------RSKISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVSVAVSTPAGLITP 488
Cdd:pfam00198  13 LTDEVDVTELLALREElkedaadeETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIGIAVATPRGLIVP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 489 IVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEk 568
Cdd:pfam00198  93 VIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRIRKRPVVVDGE- 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1716945216 569 gFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 610
Cdd:pfam00198 172 -IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 219-293 5.66e-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: 98.25  E-value: 5.66e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716945216 219 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 96-175 4.81e-24

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.38  E-value: 4.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  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 1.17e-23

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.78  E-value: 1.17e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716945216  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 220-294 1.87e-20

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 85.50  E-value: 1.87e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716945216 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 294
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 94-165 8.70e-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: 83.58  E-value: 8.70e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716945216  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 7.24e-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: 7.24e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716945216  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 ...
 221-611 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: 574.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI 300
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 301 -SAFADYRPTE--VTDLKP-QVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVK 376
Cdd:TIGR01349  82 aDAFKNYKLESsaSPAPKPsEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 377 GTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRI---------------------- 431
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIiakrlleskqtiphyyvsiecn 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 432 --------------LEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKG 497
Cdd:TIGR01349 242 vdkllalrkelnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 498 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDK-LVPADNEKGFDVASMM 576
Cdd:TIGR01349 322 LSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVaVVDNDEEKGFAVASIM 401

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1716945216 577 SVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:TIGR01349 402 SVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 212-611 4.31e-146

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 433.51  E-value: 4.31e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 212 GSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLC 291
Cdd:PLN02744  106 SSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 292 IIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGID 371
Cdd:PLN02744  186 ITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 372 LTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRIL------------------- 432
Cdd:PLN02744  266 LSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTasrllqskqtiphyyltvd 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 433 -------------------EGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNA 493
Cdd:PLN02744  341 trvdklmalrsqlnslqeaSGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDA 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 494 HIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDV 572
Cdd:PLN02744  421 DKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVIPGSGPDQYNF 500

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1716945216 573 ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PLN02744  501 ASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 220-611 2.63e-128

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 383.37  E-value: 2.63e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEKEAD 299
Cdd:PRK11856    4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 300 ISAFADYRPTEVTDLKPQVPPPtpppvaavpptpqPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTG 379
Cdd:PRK11856   83 EAAAAAEAAPEAPAPEPAPAAA-------------AAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 380 PDGRITKKDIDSFVPSKVAPAPAAVVPPTGPgmAPVPTGVFTDIPISNIRR----------------------------- 430
Cdd:PRK11856  150 PGGRITKEDVEAAAAAAAPAAAAAAAAAAAP--PAAAAEGEERVPLSGMRKaiakrmveskreiphftltdevdvtalla 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 431 ----ILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVV 506
Cdd:PRK11856  228 lrkqLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIK 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 507 SLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRV 586
Cdd:PRK11856  308 DLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE--IVVRKVMPLSLSFDHRV 385

                         410       420
                  ....*....|....*....|....*
gi 1716945216 587 VDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PRK11856  386 IDGADAARFLKALKELLENPALLLL 410
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 106-611 1.45e-79

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 261.30  E-value: 1.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 106 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGA-IICITVGKPEDIEAfknytlDSS 184
Cdd:PRK11855   16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDT-VSVGGlLAVIEAAGAAAAAA------APA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 185 AAPTPQAAPAPTPAATASPPTPSAQAPGSSYpphMQVLLPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgf 264
Cdd:PRK11855   89 AAAAPAAAAAAAPAPAAAAPAAAAAAAGGGV---VEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATM-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 265 EV--QEEGYLAKILVPEGTRdVPLGTPLcIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVaavpptpqplAPTPSA 342
Cdd:PRK11855  163 EIpsPVAGVVKEIKVKVGDK-VSVGSLL-VVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAA----------AAAPAA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 343 PCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV-----PSKVAPAPAAVVPPTGPGMAPVPT 417
Cdd:PRK11855  231 AAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVkgamsAAAAAAAAAAAAGGGGLGLLPWPK 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 418 GVFTD------IPISNIRRI-------------------------LEG-RS-----------KISVNDFIIKASALACLK 454
Cdd:PRK11855  311 VDFSKfgeietKPLSRIKKIsaanlhrswvtiphvtqfdeaditdLEAlRKqlkkeaekagvKLTMLPFFIKAVVAALKE 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 455 VPEANSSWMDT---VIRQNHvVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISN 531
Cdd:PRK11855  391 FPVFNASLDEDgdeLTYKKY-FNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISS 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 532 LGMFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PRK11855  470 LGGIGGTAFTPIINAPEVAILGVGKSQMK--PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 419-610 2.12e-79

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: 249.77  E-value: 2.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 419 VFTDIPISNIRRILEG--------RSKISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVSVAVSTPAGLITP 488
Cdd:pfam00198  13 LTDEVDVTELLALREElkedaadeETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIGIAVATPRGLIVP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 489 IVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEk 568
Cdd:pfam00198  93 VIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRIRKRPVVVDGE- 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1716945216 569 gFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 610
Cdd:pfam00198 172 -IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 221-611 1.74e-63

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: 214.60  E-value: 1.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCIIVEkeadi 300
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 301 SAFADYRPTEVTDLKPqvppptpppvaavpptpqplAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGP 380
Cdd:TIGR01347  77 GNDATAAPPAKSGEEK--------------------EETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 381 DGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPvpTGVFTDIPISNIR-----RILEGRS------------------- 436
Cdd:TIGR01347 137 TGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAA--TRPEERVKMTRLRqriaeRLKEAQNstamlttfnevdmsavmel 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 437 --------------KISVNDFIIKASALACLKVPEANSSwmdtvIRQNHVV-----DVSVAVSTPAGLITPIVFNAHIKG 497
Cdd:TIGR01347 215 rkrykeefekkhgvKLGFMSFFVKAVVAALKRFPEVNAE-----IDGDDIVykdyyDISVAVSTDRGLVVPVVRNADRMS 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 498 VETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVpADNEKgFDVASMMS 577
Cdd:TIGR01347 290 FADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQ-IEIRPMMY 367

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1716945216 578 VTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:TIGR01347 368 LALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
221-611 1.11e-56

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 196.59  E-value: 1.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIgfEV--QEEGYLAKILVPEGTrDVPLGTPLCIIVEKEA 298
Cdd:PRK05704    5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVL--EVpaPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 299 DISAFADYRPTEvtdlkpqvppptpppvaavpptPQPLAPTPSAPCPATPAGPKGrvfVSPLAKKLAVEKGIDLTQVKGT 378
Cdd:PRK05704   82 AGAAAAAAAAAA----------------------AAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVKGT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 379 GPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIR-RILEgRSKISVND--------------- 442
Cdd:PRK05704  137 GKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRkTIAE-RLLEAQNTtamlttfnevdmtpv 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 443 -----------------------FIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVE 499
Cdd:PRK05704  216 mdlrkqykdafekkhgvklgfmsFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 500 TIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVT 579
Cdd:PRK05704  296 EIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ--IVIRPMMYLA 373

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1716945216 580 LSCDHRVVDG--AVGaqWLAEFRKYLEKPITMLL 611
Cdd:PRK05704  374 LSYDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 94-604 6.70e-56

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 198.70  E-value: 6.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKIlVAEGTRDVPIGAIICItVGKPEDI 173
Cdd:TIGR02927   5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEI-RAPEDDTVEVGGVLAI-IGEPGEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 174 EAfknytldSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPH------MQVLLPALSPTMTMGTVQRWEKKVGEKLS 247
Cdd:TIGR02927  83 GS-------EPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQAggsgeaTEVKMPELGESVTEGTVTSWLKAVGDTVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 248 EGDLLAEIETDKATIGFEVQEEGYLAKILVPEgTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVA 327
Cdd:TIGR02927 156 VDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 328 AVPPTPQPLAPTPSAPCPATPAGPK----GRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSfvPSKVAPAPAA 403
Cdd:TIGR02927 235 HAAPDPPAPAPAPAKTAAPAAAAPVssgdSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLA--AAKAAEEARA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 404 VVPPTGPGMAPVPTGVFTDIP-------------ISNIRRILEGRS---------------------------------- 436
Cdd:TIGR02927 313 AAAAPAAAAAPAAPAAAAKPAepdtaklrgttqkMNRIRQITADKTieslqtsaqltqvhevdmtrvaalrarakndfle 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 437 ----KISVNDFIIKASALACLKVPEANSSWMDTV--IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLAT 510
Cdd:TIGR02927 393 kngvNLTFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAA 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 511 KAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVT---LSCDHRVV 587
Cdd:TIGR02927 473 RARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLV 552

                         570
                  ....*....|....*..
gi 1716945216 588 DGAVGAQWLAEFRKYLE 604
Cdd:TIGR02927 553 DGADAGRFLTTIKKRLE 569
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 223-611 4.32e-53

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 187.20  E-value: 4.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 223 LPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIvekeaDISA 302
Cdd:PTZ00144   49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEI-----DTGG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 303 FADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPkgrvfvSPLAKKLAVEKGIDL---TQVKGTg 379
Cdd:PTZ00144  123 APPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEP------APAAKPPPTPVARADpreTRVPMS- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 380 pdgRITKKDIDSFVPSKVApapaavvpptgpgMAPVPTgvFTDIPISNIrriLEGRSKISvNDF-------------IIK 446
Cdd:PTZ00144  196 ---RMRQRIAERLKASQNT-------------CAMLTT--FNECDMSAL---MELRKEYK-DDFqkkhgvklgfmsaFVK 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 447 ASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGT 526
Cdd:PTZ00144  254 ASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGT 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 527 FTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKP 606
Cdd:PTZ00144  334 FTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE--IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDP 411


                  ....*
gi 1716945216 607 ITMLL 611
Cdd:PTZ00144  412 ARMLL 416
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 106-611 3.56e-52

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 189.44  E-value: 3.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 106 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIIcITVGKPEDIEAfknytldssa 185
Cdd:PRK11854  118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VSTGSLI-MVFEVAGEAPA---------- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 186 aptpqaapaptPAATASPPTPSAQAPGSSyPPHMQVLLPALSptMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFE 265
Cdd:PRK11854  186 -----------AAPAAAEAAAPAAAPAAA-AGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVP 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 266 VQEEGYLAKILVPEGTRdVPLGTpLCIIVEKEADISAFAdyrPTEVTDLKPQVPPPTPPPVAAvpptpqplAPTPSAPCP 345
Cdd:PRK11854  252 APFAGTVKEIKVNVGDK-VKTGS-LIMRFEVEGAAPAAA---PAKQEAAAPAPAAAKAEAPAA--------APAAKAEGK 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 346 ATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV----PSKVAPAPAAVVPPTGPGMAPVPT---- 417
Cdd:PRK11854  319 SEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVkdavKRAEAAPAAAAAGGGGPGLLPWPKvdfs 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 418 --GVFTDIPISNIRRI-----------------------------------LEGRSKISVN----DFIIKASALACLKVP 456
Cdd:PRK11854  399 kfGEIEEVELGRIQKIsganlhrnwvmiphvtqfdkaditeleafrkqqnaEAEKRKLGVKitplVFIMKAVAAALEQMP 478

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 457 EANSSWMD---TVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLG 533
Cdd:PRK11854  479 RFNSSLSEdgqRLTLKKYV-NIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIG 557

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716945216 534 MFGIKNFSAIINPPQACILAIGASEDKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PRK11854  558 GLGTTHFTPIVNAPEVAILGVSKSAME--PVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 114-611 7.95e-52

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 187.00  E-value: 7.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 114 KEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIIC-ITVGKPEDIEAfknytldssaapTPQAA 192
Cdd:TIGR01348  22 KPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDT-LPVGGVIAtLEVGAGAQAQA------------EAKKE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 193 PAPTPAATASPPTPSAQAPGSSYPPH--MQVLLPALSpTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEG 270
Cdd:TIGR01348  89 AAPAPTAGAPAPAAQAQAAPAAGQSSgvQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 271 YLAKILVPEGTRdVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPpptpppvaavpptpQPLAPTPSAPCPATPAG 350
Cdd:TIGR01348 168 VVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAAT--------------QPEPAAAPAAAKAQAPA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 351 PKGR--------VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV--PSKVAPAPAAVVPPTGPGMAPVPTGVF 420
Cdd:TIGR01348 233 PQQAgtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVkePSVRAQAAAASAAGGAPGALPWPNVDF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 421 T------DIPISNIRRIlEGRS--------------------------------------KISVNDFIIKASALACLKVP 456
Cdd:TIGR01348 313 SkfgeveEVDMSRIRKI-SGANltrnwtmiphvthfdkaditemeafrkqqnaavekegvKLTVLHILMKAVAAALKKFP 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 457 EANSSWM---DTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLG 533
Cdd:TIGR01348 392 KFNASLDlggEQLILKKYV-NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLG 470

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716945216 534 MFGIKNFSAIINPPQACILaiGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:TIGR01348 471 GIGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 355-611 3.50e-42

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 155.45  E-value: 3.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 355 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP-SKVAPAPAAVVPPTGPGMAP---VPTGVFTDIPISNIRR 430
Cdd:PRK14843   49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPeNIENDSIKSPAQIEKVEEVPdnvTPYGEIERIPMTPMRK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 431 ILEGR--------------------------------------SKISVNDFIIKASALACLKVPEANSSWMD---TVIRQ 469
Cdd:PRK14843  129 VIAQRmvesyltaptftlnyevdmtemlalrkkvlepimeatgKKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 470 NHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQA 549
Cdd:PRK14843  209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716945216 550 CILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PRK14843  288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 237-611 4.36e-42

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 156.80  E-value: 4.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 237 RWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGtrD-VPLGTPLC-IIVEKEADISAFADYRPTEVTDL 314
Cdd:PLN02528   17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DiVKVGETLLkIMVEDSQHLRSDSLLLPTDSSNI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 315 KpqvppptpppvaavpptpqplaptpSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP 394
Cdd:PLN02528   95 V-------------------------SLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 395 SK-------VAPAPAAVVPPTGPGMAPVPTG-VFTD--IPISNIRRI--------------------------------- 431
Cdd:PLN02528  150 QKgvvkdssSAEEATIAEQEEFSTSVSTPTEqSYEDktIPLRGFQRAmvktmtaaakvphfhyveeinvdalvelkasfq 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 432 ---LEGRSKISVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAGLITPIVFNAHIKGVETIAND 504
Cdd:PLN02528  230 ennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHGLVVPNIKNVQSLSLLEITKE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 505 VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDklVPADNEKGFDV-ASMMSVTLSCD 583
Cdd:PLN02528  308 LSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPRFVDDGNVYpASIMTVTIGAD 385

                         410       420
                  ....*....|....*....|....*...
gi 1716945216 584 HRVVDGAVGAQWLAEFRKYLEKPITMLL 611
Cdd:PLN02528  386 HRVLDGATVARFCNEWKSYVEKPELLML 413
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 354-606 1.36e-32

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 127.60  E-value: 1.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 354 RVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV------PSKVAPAPAAVVPPTGPGMAPVPTGVFTDI---P 424
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGkreK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 425 ISNIR--------------------------RILEGRS------------KISVNDFIIKASALACLKVP-------EAN 459
Cdd:PRK11857   81 VAPIRkaiaramtnswsnvayvnlvneidmtKLWDLRKsvkdpvlktegvKLTFLPFIAKAILIALKEFPifaakydEAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 460 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKN 539
Cdd:PRK11857  161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716945216 540 FSAIINPPQACILAIGASEDKlvpADNEKGFDVAS-MMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKP 606
Cdd:PRK11857  236 GVPVINYPELAIAGVGAIIDK---AIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 220-358 3.04e-29

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 121.18  E-value: 3.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEAD 299
Cdd:PRK11892    4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1716945216 300 ISAFADyRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVS 358
Cdd:PRK11892   84 ASDAGA-APAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVT 141
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 219-611 4.89e-27

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 114.47  E-value: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 219 MQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPlGTPLCIIVEKEA 298
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEP-GTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 299 DISAFA-DYRPTEVTDLKPQVPPPTPPPVAAVPPtpqPLAPTPSAPCPATPagPKGRVFVSPLAKKlAVEKGIDLTQVKG 377
Cdd:PLN02226  171 AASQVTpSQKIPETTDPKPSPPAEDKQKPKVESA---PVAEKPKAPSSPPP--PKQSAKEPQLPPK-ERERRVPMTRLRK 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 378 tgpdgRITKKDIDSfvpskvapapaavvpptGPGMAPVPTgvFTDIPISNIRRI--------LEGRS-KISVNDFIIKAS 448
Cdd:PLN02226  245 -----RVATRLKDS-----------------QNTFALLTT--FNEVDMTNLMKLrsqykdafYEKHGvKLGLMSGFIKAA 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 449 ALACLKVPEANSSW-MDTVIRQNHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTF 527
Cdd:PLN02226  301 VSALQHQPVVNAVIdGDDIIYRDYV-DISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSF 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 528 TISNLGMFGIKNFSAIINPPQACILAIGAsedkLVPADNEKGFDVA--SMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEK 605
Cdd:PLN02226  380 TVSNGGVYGSLISTPIINPPQSAILGMHS----IVSRPMVVGGSVVprPMMYVALTYDHRLIDGREAVYFLRRVKDVVED 455


                  ....*.
gi 1716945216 606 PITMLL 611
Cdd:PLN02226  456 PQRLLL 461
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 219-293 5.66e-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: 98.25  E-value: 5.66e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716945216 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 3.96e-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: 95.97  E-value: 3.96e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716945216 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPLVKI 73
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 96-175 4.81e-24

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.38  E-value: 4.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  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 1.17e-23

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.78  E-value: 1.17e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716945216  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 220-294 1.87e-20

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 85.50  E-value: 1.87e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716945216 220 QVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIV 294
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAVIA 77
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 94-165 8.70e-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: 83.58  E-value: 8.70e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716945216  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 3.52e-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: 70.55  E-value: 3.52e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716945216  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 6.35e-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: 6.35e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1716945216 355 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDID 390
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 92-176 1.40e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.67  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICITV---G 168
Cdd:PRK14875    3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVAdaeV 81


                  ....*...
gi 1716945216 169 KPEDIEAF 176
Cdd:PRK14875   82 SDAEIDAF 89
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 221-305 1.77e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.28  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216 221 VLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTrDVPLGTPLCIIVEKE--- 297
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAEvsd 83


                  ....*...
gi 1716945216 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 4.63e-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: 4.63e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716945216 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 7.24e-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: 7.24e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716945216  94 VPLPSLSPTMQAGtIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 303-603 2.77e-08

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 57.21  E-value: 2.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  303 FADYRPTEVT-----DLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRV--------FVSPLAKKLAVEKG 369
Cdd:PRK12270    33 FADYGPGSTAaptaaAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAaaaaapaaPPAAAAAAAPAAAA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  370 IDLTQVKGTGPDGRITKKDIDSF-VPskvapapaavvppTGPGMAPVPTGVFTD--IPISNIRRILEGrSKISVNDFIIK 446
Cdd:PRK12270   113 VEDEVTPLRGAAAAVAKNMDASLeVP-------------TATSVRAVPAKLLIDnrIVINNHLKRTRG-GKVSFTHLIGY 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  447 ASALACLKVPEANSSWMD-----TVIRQNHV-VDVSVAVSTPAGLITPIVfnAHIKGVETIA--------NDVVSlatKA 512
Cdd:PRK12270   179 ALVQALKAFPNMNRHYAEvdgkpTLVTPAHVnLGLAIDLPKKDGSRQLVV--PAIKGAETMDfaqfwaayEDIVR---RA 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716945216  513 REGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA----------SEDKLvpadNEKGfdVASMMSVTLSC 582
Cdd:PRK12270   254 RDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefqgaSEERL----AELG--ISKVMTLTSTY 327

                          330       340
                   ....*....|....*....|.
gi 1716945216  583 DHRVVDGAVGAQWLAEFRKYL 603
Cdd:PRK12270   328 DHRIIQGAESGEFLRTIHQLL 348
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 233-293 7.63e-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: 7.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1716945216 233 GTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRdVPLGTPLCII 293
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVVI 67
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 105-129 5.45e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 35.92  E-value: 5.45e-03
                          10        20
                  ....*....|....*....|....*
gi 1716945216 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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