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Conserved domains on  [gi|1270111455|ref|NP_001344273|]
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lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial isoform 2 [Mus musculus]

Protein Classification

lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex( domain architecture ID 1003376)

lipoamide acyltransferase component (E2) of branched-chain alpha-keto acid dehydrogenase complex that catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2)

CATH:  3.30.559.10
EC:  2.3.1.168
Gene Ontology:  GO:0043754|GO:0016407|GO:0031625|GO:0031405|GO:0009083

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02528 super family cl33511
2-oxoisovalerate dehydrogenase E2 component
 2-301 1.16e-134

2-oxoisovalerate dehydrogenase E2 component


The actual alignment was detected with superfamily member PLN02528:

Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 387.92  E-value: 1.16e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLeKQTGAILPPSPKSEITPPPPQPKDRTFPTPIAKppvfTGKDRTEPVTGFQKA 81
Cdd:PLN02528  122 QYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSSAEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASH 161
Cdd:PLN02528  197 MVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSH 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 162 NIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGA 241
Cdd:PLN02528  277 NIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIA 356

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 242 LGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK 301
Cdd:PLN02528  357 LGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 2-301 1.16e-134

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 387.92  E-value: 1.16e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLeKQTGAILPPSPKSEITPPPPQPKDRTFPTPIAKppvfTGKDRTEPVTGFQKA 81
Cdd:PLN02528  122 QYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSSAEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASH 161
Cdd:PLN02528  197 MVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSH 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 162 NIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGA 241
Cdd:PLN02528  277 NIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIA 356

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 242 LGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK 301
Cdd:PLN02528  357 LGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 86-297 1.21e-96

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: 283.67  E-value: 1.21e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  86 MSAAL-KIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIG 164
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 165 IAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGA 244
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1270111455 245 IKALPRFDQkGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 297
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 2-298 2.23e-54

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


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 185.08  E-value: 2.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAIlPPSPKSEITPPPPQPkdrtfPTPIAKPPVFtGKDRTEPVTGFQKA 81
Cdd:TIGR01348 257 EFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRA-QAAAASAAGGAPGAL-----PWPNVDFSKF-GEVEEVDMSRIRKI 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAA-LKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKAS 160
Cdd:TIGR01348 330 SGANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKY 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 161 HNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIg 240
Cdd:TIGR01348 410 VNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI- 488

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 241 aLGAIKAL--PRFDQKGDVYKaQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:TIGR01348 489 -LGVSKSGmePVWNGKEFEPR-LMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 2-301 1.16e-134

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 387.92  E-value: 1.16e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLeKQTGAILPPSPKSEITPPPPQPKDRTFPTPIAKppvfTGKDRTEPVTGFQKA 81
Cdd:PLN02528  122 QYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSSAEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASH 161
Cdd:PLN02528  197 MVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSH 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 162 NIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGA 241
Cdd:PLN02528  277 NIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIA 356

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 242 LGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK 301
Cdd:PLN02528  357 LGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 2-298 1.06e-117

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 349.12  E-value: 1.06e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLE-KQTGAILPPSPKSEITPPPPQPKdrtfPTPIAKPPVFtGKDRTEPVTGFQK 80
Cdd:PRK11855  255 ELGVDLSQVKGTGKKGRITKEDVQAFVKgAMSAAAAAAAAAAAAGGGGLGLL----PWPKVDFSKF-GEIETKPLSRIKK 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  81 AMVKTMSAAL-KIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKA 159
Cdd:PRK11855  330 ISAANLHRSWvTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKK 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 160 SHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAI 239
Cdd:PRK11855  410 YFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAI 489

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111455 240 GALGAIKALPrFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:PRK11855  490 LGVGKSQMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 86-297 1.21e-96

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: 283.67  E-value: 1.21e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  86 MSAAL-KIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIG 164
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 165 IAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGA 244
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1270111455 245 IKALPRFDQkGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 297
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 2-299 1.50e-93

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 282.84  E-value: 1.50e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEKQtgailppspkseitpppPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKA 81
Cdd:PRK11856  137 ELGVDLSTVKGSGPGGRITKEDVEAAAAAA-----------------APAAAAAAAAAAAPPAAAAEGEERVPLSGMRKA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAA-LKIPHFGYCDEIDLTQLVKLREELKPVAlargIKLSFMPFFLKAASLGLLQFPILNASVDEncQNITYKAS 160
Cdd:PRK11856  200 IAKRMVESkREIPHFTLTDEVDVTALLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKY 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 161 HNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIG 240
Cdd:PRK11856  274 VNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAIL 353

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111455 241 ALGAIKALPRFdQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD 299
Cdd:PRK11856  354 GVGAIVERPVV-VDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 2-293 1.99e-67

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 212.73  E-value: 1.99e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAilpPSPKSEITPPPPQPKDRTfPTPIAKPPVFTGKdrTEPVTGFQKA 81
Cdd:PRK11857   14 KLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEGK--REKVAPIRKA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAALK-IPHFGYCDEIDLTQLVKLREELK-PVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKA 159
Cdd:PRK11857   88 IARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSELVYPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 160 SHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAI 239
Cdd:PRK11857  168 TLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAI 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1270111455 240 GALGAIKALPRFdQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENP 293
Cdd:PRK11857  248 AGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 2-292 1.83e-59

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 200.23  E-value: 1.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEK-----QTGAILPPSPKSEITPPPpqpkdrtfpTPIAKPPVFtGKDRTEPVT 76
Cdd:PRK11854  340 EFGVNLAKVKGTGRKGRILKEDVQAYVKDavkraEAAPAAAAAGGGGPGLLP---------WPKVDFSKF-GEIEEVELG 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  77 GFQKAMVKTMSAAL-KIPHFGYCDEIDLTQLVKLREELKPVALAR--GIKLSFMPFFLKAASLGLLQFPILNASVDENCQ 153
Cdd:PRK11854  410 RIQKISGANLHRNWvMIPHVTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQ 489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 154 NITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVIL 233
Cdd:PRK11854  490 RLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVN 569

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111455 234 PPEVAIGALGAIKALPRFDQKGDVYKaQIMNVSWSADHRVIDGATMSRFSNLWKSYLEN 292
Cdd:PRK11854  570 APEVAILGVSKSAMEPVWNGKEFAPR-LMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 2-298 2.23e-54

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


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 185.08  E-value: 2.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAIlPPSPKSEITPPPPQPkdrtfPTPIAKPPVFtGKDRTEPVTGFQKA 81
Cdd:TIGR01348 257 EFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRA-QAAAASAAGGAPGAL-----PWPNVDFSKF-GEVEEVDMSRIRKI 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAA-LKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKAS 160
Cdd:TIGR01348 330 SGANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKY 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 161 HNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIg 240
Cdd:TIGR01348 410 VNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI- 488

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 241 aLGAIKAL--PRFDQKGDVYKaQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:TIGR01348 489 -LGVSKSGmePVWNGKEFEPR-LMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 2-295 3.25e-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: 177.51  E-value: 3.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAILPPSPkseiTPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKA 81
Cdd:TIGR02927 278 DKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAA----PAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQI 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAALKI-PHFGYCDEIDLTQLVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKA 159
Cdd:TIGR02927 354 TADKTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHD 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 160 SHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAI 239
Cdd:TIGR02927 434 VEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAI 513

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 240 GALGAIKALPRF--DQKGDVYKA--QIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAF 295
Cdd:TIGR02927 514 LGTGAIVKRPRVikDEDGGESIAirSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 2-298 3.92e-50

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: 171.52  E-value: 3.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLekqtgailPPSPKseitPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKA 81
Cdd:TIGR01349 152 EKGIDLSAVAGSGPNGRIVKKDIESFV--------PQSPA----SANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKI 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  82 MVKTMSAALK-IPHFGYCDEIDLTQLVKLREELKPVALARgIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKAS 160
Cdd:TIGR01349 220 IAKRLLESKQtIPHYYVSIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKN 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 161 HNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIG 240
Cdd:TIGR01349 297 VDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACIL 376

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 241 ALGAI--KALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:TIGR01349 377 AVGAVedVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 1-300 7.24e-50

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: 169.91  E-value: 7.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   1 MENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAILPPSPKSEitppppqpkdrtfptpiAKPPVFTGKDRTEPVTGFQK 80
Cdd:TIGR01347 122 KEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAA-----------------AAPAAATRPEERVKMTRLRQ 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  81 AMVKTM-----SAALkIPHFgycDEIDLTQLVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqN 154
Cdd:TIGR01347 185 RIAERLkeaqnSTAM-LTTF---NEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--D 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 155 ITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILP 234
Cdd:TIGR01347 259 IVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINP 338

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111455 235 PEVAIGALGAIKALPrFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 300
Cdd:TIGR01347 339 PQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-300 2.00e-48

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 166.16  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEKqtgailPPSPKSEITPPPPQPkdrtfptpiakPPVFTGkDRTE---PVTGF 78
Cdd:PRK05704  125 ENGLDASAVKGTGKGGRVTKEDVLAALAA------AAAAPAAPAAAAPAA-----------APAPLG-ARPEervPMTRL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  79 QK-------------AMVKTmsaalkiphFgycDEIDLTQLVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPIL 144
Cdd:PRK05704  187 RKtiaerlleaqnttAMLTT---------F---NEVDMTPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEV 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 145 NASVDENcqNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNigsiG 224
Cdd:PRK05704  255 NASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----G 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 225 GTY----AKPVILPPEVAIgaLG--AIKALPrFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:PRK05704  329 GVFgslmSTPIINPPQSAI--LGmhKIKERP-VAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405


                  ..
gi 1270111455 299 DL 300
Cdd:PRK05704  406 DL 407
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 29-300 6.00e-47

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 162.54  E-value: 6.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  29 EKQTGAILPPSPKSEITPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQK--AMVKTMSAALK--------IPHFgyc 98
Cdd:PTZ00144  142 PEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRETRVPmsRMRQRIAERLKasqntcamLTTF--- 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  99 DEIDLTQLVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENCqnITYKASHNIGIAMDTELGLIVPN 177
Cdd:PTZ00144  219 NECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPV 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 178 VKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALP--RFDQkg 255
Cdd:PTZ00144  297 IRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPvvVGNE-- 374

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1270111455 256 dVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 300
Cdd:PTZ00144  375 -IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 1-298 1.37e-35

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 131.18  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   1 MENNIKLSEVVGSGKDGRILKEDILSFLekqtgailpPSPKSEITPPPPQPKDRTFPTPIAKPPvfTGKDRTEPVTGFQK 80
Cdd:PRK14843   60 LEHNIAWQEIQGTGHRGKIMKKDVLALL---------PENIENDSIKSPAQIEKVEEVPDNVTP--YGEIERIPMTPMRK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  81 AMVKTMSAA-LKIPHFGYCDEIDLTQLVKLREE-LKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYK 158
Cdd:PRK14843  129 VIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITH 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 159 ASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVA 238
Cdd:PRK14843  209 NYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSA 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 239 IGALGAIKALPRFdQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:PRK14843  289 ILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 2-298 1.89e-34

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 131.13  E-value: 1.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDILSFLEkqtgailppSPKSEITPPPPQPKDRTfptpiakppvftGKDRTE-PVTGFQK 80
Cdd:PLN02744  261 DNNVPLSSIKGTGPDGRIVKADIEDYLA---------SGGKGATAPPSTDSKAP------------ALDYTDiPNTQIRK 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  81 AMVKTM-SAALKIPHFGYCDEIDLTQLVKLREELKPVALARGIK-LSFMPFFLKAASLGLLQFPILNAS-VDENcqnITY 157
Cdd:PLN02744  320 VTASRLlQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDY---IRQ 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 158 KASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGS-IGGTYAKPVILPPE 236
Cdd:PLN02744  397 YHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQ 476

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111455 237 VAIGALG-AIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 298
Cdd:PLN02744  477 SAILAVGsAEKRVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 37-300 1.52e-33

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 127.56  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  37 PPS-----PKSEITPPPPQPKDRTFPTP---IAKPPVFTGKDRTE--PVTGFQKAMVKTMSAALK-IPHFGYCDEIDLTQ 105
Cdd:PLN02226  191 PPAedkqkPKVESAPVAEKPKAPSSPPPpkqSAKEPQLPPKERERrvPMTRLRKRVATRLKDSQNtFALLTTFNEVDMTN 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 106 LVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTELGLIVPNVKNVQVR 184
Cdd:PLN02226  271 LMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKM 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455 185 SVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRFdQKGDVYKAQIMN 264
Cdd:PLN02226  349 NFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMY 427

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1270111455 265 VSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 300
Cdd:PLN02226  428 VALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 37-282 2.01e-15

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 76.47  E-value: 2.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455   37 PPSPKSEITPPPPQPKDRTFPTPIAKPPVftgKDRTEPVTGFQKAMVKTMSAALKIPhfgycdeidlTQL------VKLR 110
Cdd:PRK12270    85 KPAAAAAAAAAPAAPPAAAAAAAPAAAAV---EDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLL 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  111 EELKPV-----ALARGIKLSFMPFFLKAASLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTE-----LGLIVPNV 178
Cdd:PRK12270   152 IDNRIVinnhlKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAI 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111455  179 KNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRF-----DQ 253
Cdd:PRK12270   232 KGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFqgaseER 311

                          250       260
                   ....*....|....*....|....*....
gi 1270111455  254 KGDVYKAQIMNVSWSADHRVIDGATMSRF 282
Cdd:PRK12270   312 LAELGISKVMTLTSTYDHRIIQGAESGEF 340
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 2-25 5.10e-07

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: 45.37  E-value: 5.10e-07
                          10        20
                  ....*....|....*....|....
gi 1270111455   2 ENNIKLSEVVGSGKDGRILKEDIL 25
Cdd:pfam02817  13 ELGIDLSDVKGTGPGGRITKEDVE 36
 
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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