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Conserved domains on  [gi|1716962988|ref|NP_001358968|]
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dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial isoform 10 [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 ...
 93-542 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: 675.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  93 KVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPED 172
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 173 IE-AFKNYTLDSSAAPTPQAAPAptpaataspptpsaqAPgssyPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKGRVF 251
Cdd:TIGR01349  81 VAdAFKNYKLESSASPAPKPSEI---------------AP----TAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 252 VSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA 328
Cdd:TIGR01349 142 ASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 329 QRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV 408
Cdd:TIGR01349 222 KRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISV 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 409 AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAS 488
Cdd:TIGR01349 302 AVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAV 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1716962988 489 EDK-LVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:TIGR01349 382 EDVaVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 93-542 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: 675.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  93 KVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPED 172
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 173 IE-AFKNYTLDSSAAPTPQAAPAptpaataspptpsaqAPgssyPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKGRVF 251
Cdd:TIGR01349  81 VAdAFKNYKLESSASPAPKPSEI---------------AP----TAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 252 VSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA 328
Cdd:TIGR01349 142 ASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 329 QRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV 408
Cdd:TIGR01349 222 KRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISV 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 409 AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAS 488
Cdd:TIGR01349 302 AVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAV 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1716962988 489 EDK-LVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:TIGR01349 382 EDVaVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 24-542 1.05e-177

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 511.71  E-value: 1.05e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  24 ALQEVPGTPRVTSRSGPaparrnSVTTGYGGVRALCGWTPSSGATPRNRLLLQLLGS----PGRRYYS---LPPHQKVPL 96
Cdd:PLN02744   44 DIAKRRGYPPLERRSQP------KVSSLGLFGSNISRTARKNGSPMTGSGLFKSLSSsqmqSARGFSSssdLPPHQEIGM 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  97 PSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAF 176
Cdd:PLN02744  118 PSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKF 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 177 KNYTLDSSAAPTPQaapaptpaataspptpsaqAPGSSYPPHMQVAAVPPTPqplAPTPSAPCPATPAGPKGRVFVSPLA 256
Cdd:PLN02744  198 KDYKPSSSAAPAAP-------------------KAKPSPPPPKEEEVEKPAS---SPEPKASKPSAPPSSGDRIFASPLA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 257 KKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQ 336
Cdd:PLN02744  256 RKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQ 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 337 TIPHYYLSIDVNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPA 414
Cdd:PLN02744  331 TIPHYYLTVDTRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTEN 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 415 GLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLV 493
Cdd:PLN02744  411 GLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVI 490

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1716962988 494 PADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PLN02744  491 PGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 331-541 8.35e-95

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: 8.35e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 331 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 407
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 408 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 487
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962988 488 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 541
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 92-165 2.33e-24

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 96.32  E-value: 2.33e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716962988  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 94-165 2.48e-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: 85.12  E-value: 2.48e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962988  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICI 165
Cdd:COG0508     5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGD-TVPVGAVIAV 75
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 93-542 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: 675.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  93 KVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPED 172
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 173 IE-AFKNYTLDSSAAPTPQAAPAptpaataspptpsaqAPgssyPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKGRVF 251
Cdd:TIGR01349  81 VAdAFKNYKLESSASPAPKPSEI---------------AP----TAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 252 VSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVA---PAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA 328
Cdd:TIGR01349 142 ASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPAsanQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 329 QRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV 408
Cdd:TIGR01349 222 KRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISV 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 409 AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAS 488
Cdd:TIGR01349 302 AVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAV 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1716962988 489 EDK-LVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:TIGR01349 382 EDVaVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 24-542 1.05e-177

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 511.71  E-value: 1.05e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  24 ALQEVPGTPRVTSRSGPaparrnSVTTGYGGVRALCGWTPSSGATPRNRLLLQLLGS----PGRRYYS---LPPHQKVPL 96
Cdd:PLN02744   44 DIAKRRGYPPLERRSQP------KVSSLGLFGSNISRTARKNGSPMTGSGLFKSLSSsqmqSARGFSSssdLPPHQEIGM 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  97 PSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAF 176
Cdd:PLN02744  118 PSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKF 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 177 KNYTLDSSAAPTPQaapaptpaataspptpsaqAPGSSYPPHMQVAAVPPTPqplAPTPSAPCPATPAGPKGRVFVSPLA 256
Cdd:PLN02744  198 KDYKPSSSAAPAAP-------------------KAKPSPPPPKEEEVEKPAS---SPEPKASKPSAPPSSGDRIFASPLA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 257 KKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSkvapaPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQ 336
Cdd:PLN02744  256 RKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLAS-----GGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQ 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 337 TIPHYYLSIDVNMGEVLLVRKELNKILE--GRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPA 414
Cdd:PLN02744  331 TIPHYYLTVDTRVDKLMALRSQLNSLQEasGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTEN 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 415 GLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNL-GMFGIKNFSAIINPPQACILAIGASEDKLV 493
Cdd:PLN02744  411 GLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRVI 490

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1716962988 494 PADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PLN02744  491 PGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 96-542 6.14e-153

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 443.46  E-value: 6.14e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  96 LPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICiTVGKPEDIEA 175
Cdd:PRK11856    7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIA-VIEEEGEAEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 176 fknytldssaaptpqaapaptpaataspptpsaqAPGSSYPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPL 255
Cdd:PRK11856   85 ----------------------------------AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 256 AKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPgmAPVPTGVFTDIPISNIRRVIAQRLMQSK 335
Cdd:PRK11856  131 VRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAP--PAAAAEGEERVPLSGMRKAIAKRMVESK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 336 QTIPHYYLSIDVNMGEVLLVRKELNKILEgrsKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAG 415
Cdd:PRK11856  209 REIPHFTLTDEVDVTALLALRKQLKAIGV---KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGG 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 416 LITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPA 495
Cdd:PRK11856  286 LIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1716962988 496 DNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PRK11856  366 DGE--IVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 331-541 8.35e-95

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: 8.35e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 331 LMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT--VIRQNHVVDVS 407
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 408 VAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA 487
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962988 488 SEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITML 541
Cdd:pfam00198 161 IRKRPVVVDGE--IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 106-542 3.65e-84

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 271.31  E-value: 3.65e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 106 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGA-IICITVGKPEDIEAfknytldss 184
Cdd:PRK11855  133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSlLVVIEVAAAAPAAA--------- 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 185 aaptpqaapaptpaataspptpsaQAPGSSYPPHMQVAAVPPTPQPlAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKG 264
Cdd:PRK11855  203 ------------------------AAPAAAAPAAAAAAAPAPAPAA-AAAPAAAAPAAAAAPGKAPHASPAVRRLARELG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 265 IDLTQVKGTGPDGRITKKDIDSFV-----PSKVAPAPAAVVPPTGPGMAPVPTGVFTD------IPISNIRRVIAQRLMQ 333
Cdd:PRK11855  258 VDLSQVKGTGKKGRITKEDVQAFVkgamsAAAAAAAAAAAAGGGGLGLLPWPKVDFSKfgeietKPLSRIKKISAANLHR 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 334 SKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS-KISVNDFIIKASALACLKVPEANSSWMDT---VIRQNHVvDVSVA 409
Cdd:PRK11855  338 SWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGvKLTMLPFFIKAVVAALKEFPVFNASLDEDgdeLTYKKYF-NIGFA 416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 410 VSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASE 489
Cdd:PRK11855  417 VDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQ 496

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1716962988 490 DKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PRK11855  497 MK--PVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 94-542 4.07e-69

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: 227.69  E-value: 4.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICITvgkpedi 173
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAIL------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 174 eafknytldssaaptpqaapaptpaataspptpsaqAPGSSYPPHmQVAAVPPTPQPLAPTPSAPCPATPAGPKGrvfVS 253
Cdd:TIGR01347  75 ------------------------------------EEGNDATAA-PPAKSGEEKEETPAASAAAAPTAAANRPS---LS 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 254 PLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMApvPTGVFTDIPISNIRRVIAQRLMQ 333
Cdd:TIGR01347 115 PAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAA--ATRPEERVKMTRLRQRIAERLKE 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 334 SKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSwmdtvIRQNHVV-----DV 406
Cdd:TIGR01347 193 AQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHgvKLGFMSFFVKAVVAALKRFPEVNAE-----IDGDDIVykdyyDI 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 407 SVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIG 486
Cdd:TIGR01347 268 SVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMH 347

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1716962988 487 ASEDKLVpADNEKgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:TIGR01347 348 GIKERPV-AVNGQ-IEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
97-542 2.68e-66

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 220.48  E-value: 2.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  97 PSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICItvgkpedIEAf 176
Cdd:PRK05704    8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGR-------IDE- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 177 knytldssaaptpqaapaptpaataspptpsAQAPGSSYPphmqvAAVPPTPQPLAPTPSAPCPATPAGPKGrvfVSPLA 256
Cdd:PRK05704   79 -------------------------------GAAAGAAAA-----AAAAAAAAAAAPAQAQAAAAAEQSNDA---LSPAA 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 257 KKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQ 336
Cdd:PRK05704  120 RKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQN 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 337 TIphyylSI-----DVNMGEVLLVRKELNKILEGR--SKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVA 409
Cdd:PRK05704  200 TT-----AMlttfnEVDMTPVMDLRKQYKDAFEKKhgVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIA 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 410 VSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASE 489
Cdd:PRK05704  275 VGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIK 354

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1716962988 490 DKLVPADNEkgFDVASMMSVTLSCDHRVVDG--AVGaqWLAEFRKYLEKPITMLL 542
Cdd:PRK05704  355 ERPVAVNGQ--IVIRPMMYLALSYDHRIIDGkeAVG--FLVTIKELLEDPERLLL 405
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 106-542 4.20e-62

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 215.25  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 106 GTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICItvgkpedieaFKnytldssa 185
Cdd:PRK11854  219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMR----------FE-------- 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 186 aptpqaapaptpaataspptPSAQAPGSSypPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKGR------VFVSPLAKKL 259
Cdd:PRK11854  280 --------------------VEGAAPAAA--PAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFaendayVHATPLVRRL 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 260 AVEKGIDLTQVKGTGPDGRITKKDIDSFV----PSKVAPAPAAVVPPTGPGMAPVPT------GVFTDIPISNIRRVIAQ 329
Cdd:PRK11854  338 AREFGVNLAKVKGTGRKGRILKEDVQAYVkdavKRAEAAPAAAAAGGGGPGLLPWPKvdfskfGEIEEVELGRIQKISGA 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 330 RLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS---KISVNDFIIKASALACLKVPEANSSWMD---TVIRQNHV 403
Cdd:PRK11854  418 NLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKlgvKITPLVFIMKAVAAALEQMPRFNSSLSEdgqRLTLKKYV 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 404 vDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACIL 483
Cdd:PRK11854  498 -NIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAIL 576

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1716962988 484 AIGASEDKlvPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PRK11854  577 GVSKSAME--PVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 94-542 1.38e-59

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 202.99  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICI--TVGKPE 171
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSEidTGGAPP 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 172 DIEAFKnytldssaaptpqaapaptpaataspptpSAQAPGSSYPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPkgrvf 251
Cdd:PTZ00144  126 AAAPAA-----------------------------AAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEP----- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 252 vSPLAKKLAvekgidlTQVKGTGPDGritkkdidsfvpskvapapaavvpptgpgmapvptgvfTDIPISNIRRVIAQRL 331
Cdd:PTZ00144  172 -APAAKPPP-------TPVARADPRE--------------------------------------TRVPMSRMRQRIAERL 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 332 MQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVA 409
Cdd:PTZ00144  206 KASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHgvKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVA 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 410 VSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASE 489
Cdd:PTZ00144  286 VATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIK 365

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1716962988 490 DKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PTZ00144  366 KRPVVVGNE--IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 250-542 6.91e-59

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 198.98  E-value: 6.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 250 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVP-SKVAPAPAAVVPPTGPGMAP---VPTGVFTDIPISNIRR 325
Cdd:PRK14843   49 VRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPeNIENDSIKSPAQIEKVEEVPdnvTPYGEIERIPMTPMRK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 326 VIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGR-SKISVNDFIIKASALACLKVPEANSSWMD---TVIRQ 400
Cdd:PRK14843  129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATgKKTTVTDLLSLAVVKTLMKHPYINASLTEdgkTIITH 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 401 NHVvDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQA 480
Cdd:PRK14843  209 NYV-NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNS 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962988 481 CILAIGASEDKLVPADNEkgFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PRK14843  288 AILGVSSTIEKPVVVNGE--IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 114-542 3.06e-56

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: 197.40  E-value: 3.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 114 KEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICITVGKpedieafknytldssaaptpqaap 193
Cdd:TIGR01348 138 KVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVA------------------------ 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 194 aptpaataSPPTPSAQAPGSSYPPhmqvAAVPPTPQPLAPTPSAPCPATPAGPKGR--------VFVSPLAKKLAVEKGI 265
Cdd:TIGR01348 193 --------GSTPATAPAPASAQPA----AQSPAATQPEPAAAPAAAKAQAPAPQQAgtqnpakvDHAAPAVRRLAREFGV 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 266 DLTQVKGTGPDGRITKKDIDSFV--PSKVAPAPAAVVPPTGPGMAPVPTGVFT------DIPISNIRRVIAQRLMQSKQT 337
Cdd:TIGR01348 261 DLSAVKGTGIKGRILREDVQRFVkePSVRAQAAAASAAGGAPGALPWPNVDFSkfgeveEVDMSRIRKISGANLTRNWTM 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 338 IPH--YYLSIDVNMGEVLLVRKELNKILEGrSKISVNDFIIKASALACLKVPEANSSWM---DTVIRQNHVvDVSVAVST 412
Cdd:TIGR01348 341 IPHvtHFDKADITEMEAFRKQQNAAVEKEG-VKLTVLHILMKAVAAALKKFPKFNASLDlggEQLILKKYV-NIGVAVDT 418

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 413 PAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILaiGASEDKL 492
Cdd:TIGR01348 419 PNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAIL--GVSKSGM 496

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1716962988 493 VPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:TIGR01348 497 EPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 94-535 3.33e-51

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: 184.45  E-value: 3.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  94 VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEgTRDVPIGAIICItVGkpedi 173
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAI-IG----- 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 174 eafknytlDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPkgrvFVS 253
Cdd:TIGR02927 202 --------DANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGP----YVT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 254 PLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSfvPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIP-------------I 320
Cdd:TIGR02927 270 PLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLA--AAKAAEEARAAAAAPAAAAAPAAPAAAAKPAepdtaklrgttqkM 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 321 SNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRS--KISVNDFIIKASALACLKVPEANSSWMDTV- 397
Cdd:TIGR02927 348 NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNgvNLTFLPFFVQAVTEALKAHPNVNASYNAETk 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 398 -IRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIIN 476
Cdd:TIGR02927 428 eVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILN 507

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962988 477 PPQACILAIGASEDKLVPADNEKGFDVASMMSVT---LSCDHRVVDGAVGAQWLAEFRKYLE 535
Cdd:TIGR02927 508 PPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCylpLTYDHRLVDGADAGRFLTTIKKRLE 569
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 110-542 1.55e-48

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 173.37  E-value: 1.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 110 RWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGtrDVpigaiicITVGKPedieAFKNYTLDSSAAPtp 189
Cdd:PLN02528   17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DI-------VKVGET----LLKIMVEDSQHLR-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 190 qaapaptpaataspptpsaqaPGSSYPPHMQVAAVpptpqplaptpSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQ 269
Cdd:PLN02528   82 ---------------------SDSLLLPTDSSNIV-----------SLAESDERGSNLSGVLSTPAVRHLAKQYGIDLND 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 270 VKGTGPDGRITKKDIDSFVPSK-VAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIA----QRLMQSKQT----IPH 340
Cdd:PLN02528  130 ILGTGKDGRVLKEDVLKYAAQKgVVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPlrgfQRAMVKTMTaaakVPH 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 341 YYLSIDVNMGEVLLVRKELNKI-LEGRSKISVNDFIIKASALACLKVPEANSSW----MDTVIRQNHvvDVSVAVSTPAG 415
Cdd:PLN02528  210 FHYVEEINVDALVELKASFQENnTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFneetSEIRLKGSH--NIGVAMATEHG 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 416 LITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDklVPA 495
Cdd:PLN02528  288 LVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQK--VPR 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1716962988 496 DNEKGFDV-ASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PLN02528  366 FVDDGNVYpASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 249-537 8.21e-41

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 149.56  E-value: 8.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 249 RVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV------PSKVAPAPAAVVPPTGPGMAPVPTGVFTDI---P 319
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGkreK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 320 ISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKE-LNKILEGRS-KISVNDFIIKASALACLKVP-------EAN 390
Cdd:PRK11857   81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSvKDPVLKTEGvKLTFLPFIAKAILIALKEFPifaakydEAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 391 SSwmdtvIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKN 470
Cdd:PRK11857  161 SE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716962988 471 FSAIINPPQACILAIGASEDKlvpADNEKGFDVAS-MMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKP 537
Cdd:PRK11857  236 GVPVINYPELAIAGVGAIIDK---AIVKNGQIVAGkVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 96-253 1.79e-26

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 112.32  E-value: 1.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  96 LPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEA 175
Cdd:PRK11892    7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716962988 176 fknytldssaaptpqaapaptpaATASPPTPSAQAPGSSYPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVS 253
Cdd:PRK11892   87 -----------------------AGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVT 141
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 96-542 4.73e-25

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 108.30  E-value: 4.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  96 LPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITvgKPEDiea 175
Cdd:PLN02226   96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIIS--KSED--- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 176 fknytldssaaptpqaapaptpaataspptpsaqapgssypphmqvAAVPPTPQPLAPTPSAPCPATPA--GPKGRVFVS 253
Cdd:PLN02226  171 ----------------------------------------------AASQVTPSQKIPETTDPKPSPPAedKQKPKVESA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 254 PLAKKlavekgidlTQVKGTGPDGRITKKDidsfvpskvapapaavvpptgPGMAPVPTGvfTDIPISNIRRVIAQRLMQ 333
Cdd:PLN02226  205 PVAEK---------PKAPSSPPPPKQSAKE---------------------PQLPPKERE--RRVPMTRLRKRVATRLKD 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 334 SKQTIPHYYLSIDVNMGEVLLVRKEL-NKILEGRS-KISVNDFIIKASALACLKVPEANSSW-MDTVIRQNHVvDVSVAV 410
Cdd:PLN02226  253 SQNTFALLTTFNEVDMTNLMKLRSQYkDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIdGDDIIYRDYV-DISIAV 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988 411 STPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGAsed 490
Cdd:PLN02226  332 GTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHS--- 408

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1716962988 491 kLVPADNEKGFDVA--SMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL 542
Cdd:PLN02226  409 -IVSRPMVVGGSVVprPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 92-165 2.33e-24

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 96.32  E-value: 2.33e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716962988  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 94-165 2.48e-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: 85.12  E-value: 2.48e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962988  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 1.14e-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: 71.70  E-value: 1.14e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962988  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 ...
 250-285 5.38e-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: 5.38e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1716962988 250 VFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDID 285
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 92-176 8.88e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 73.05  E-value: 8.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  92 QKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTrDVPIGAIICITV---G 168
Cdd:PRK14875    3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVAdaeV 81


                  ....*...
gi 1716962988 169 KPEDIEAF 176
Cdd:PRK14875   82 SDAEIDAF 89
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 94-165 3.80e-10

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


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 56.07  E-value: 3.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1716962988  94 VPLPSLSPTMQAGtIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRdVPIGAIICI 165
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 209-534 7.08e-07

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 52.20  E-value: 7.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  209 QAPGSSYPPHMQVAAVPPTPQPLAPTPSAPCPATPAGPKgrvfvSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFv 288
Cdd:PRK12270    62 PAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPP-----AAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASL- 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  289 pskvapapaavvpptgpgmaPVPTGV-FTDIP----ISNiRRVIAQRLmqsKQTiphyylsidvnmgevllvrkelnkil 363
Cdd:PRK12270   136 --------------------EVPTATsVRAVPakllIDN-RIVINNHL---KRT-------------------------- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  364 eGRSKISVNDFIIKASALACLKVPEANSSWMD-----TVIRQNHV-VDVSVAVSTPAGLITPIVfnAHIKGVETIA---- 433
Cdd:PRK12270   166 -RGGKVSFTHLIGYALVQALKAFPNMNRHYAEvdgkpTLVTPAHVnLGLAIDLPKKDGSRQLVV--PAIKGAETMDfaqf 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716962988  434 ----NDVVSlatKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGA----------SEDKLvpadNEK 499
Cdd:PRK12270   243 waayEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefqgaSEERL----AEL 315

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1716962988  500 GfdVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYL 534
Cdd:PRK12270   316 G--ISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 105-129 3.65e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 36.30  E-value: 3.65e-03
                          10        20
                  ....*....|....*....|....*
gi 1716962988 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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