NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|260898739|ref|NP_001159630|]
View 

pyruvate dehydrogenase protein X component, mitochondrial isoform 3 precursor [Homo sapiens]

Protein Classification

2-oxo acid dehydrogenase subunit E2( domain architecture ID 10446075)

2-oxo acid dehydrogenase subunit E2 similar to the dihydrolipoyllysine-residue acetyltransferase and lipoamide acyltransferase components of pyruvate dehydrogenase and branched-chain alpha-keto acid dehydrogenase complexes, respectively

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 109-273 6.07e-65

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: 202.00  E-value: 6.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  109 ILAKIV-----QMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPE 181
Cdd:pfam00198  45 FLVKAValalkKFPELNASWDGEEGEivYKKYVNIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  182 EYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEegnakLQQRQLITVTMSSDSRVVDDELATRFLK 261
Cdd:pfam00198 125 DLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRIRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLN 199

                         170
                  ....*....|..
gi 260898739  262 SFKANLENPIRL 273
Cdd:pfam00198 200 TLKELLENPELL 211
PRK11892 super family cl36077
pyruvate dehydrogenase subunit beta; Provisional
 56-114 1.09e-25

pyruvate dehydrogenase subunit beta; Provisional


The actual alignment was detected with superfamily member PRK11892:

Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.00  E-value: 1.09e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:PRK11892   2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKIL 60
 
Name Accession Description Interval E-value
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 109-273 6.07e-65

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: 202.00  E-value: 6.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  109 ILAKIV-----QMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPE 181
Cdd:pfam00198  45 FLVKAValalkKFPELNASWDGEEGEivYKKYVNIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  182 EYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEegnakLQQRQLITVTMSSDSRVVDDELATRFLK 261
Cdd:pfam00198 125 DLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRIRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLN 199

                         170
                  ....*....|..
gi 260898739  262 SFKANLENPIRL 273
Cdd:pfam00198 200 TLKELLENPELL 211
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-273 1.83e-63

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 204.64  E-value: 1.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDG--------------------------- 108
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGtvakllveegdvvpvgsviavieeege 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739     --------------------------------------------------------------------------------
Cdd:PRK11856  82 aeaaaaaeaapeapapepapaaaaaaaaapaaaaapaapaaaaakaspavrklarelgvdlstvkgsgpggritkedvea 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739     --------------------------------------------------------------------------------
Cdd:PRK11856 162 aaaaaapaaaaaaaaaaappaaaaegeervplsgmrkaiakrmveskreiphftltdevdvtallalrkqlkaigvkltv 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 109 --ILAKIV-----QMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPE 181
Cdd:PRK11856 242 tdFLIKAValalkKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 182 EYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRF 259
Cdd:PRK11856 322 ELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGADAARF 394

                        410
                 ....*....|....
gi 260898739 260 LKSFKANLENPIRL 273
Cdd:PRK11856 395 LKALKELLENPALL 408
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 115-273 2.97e-59

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: 194.24  E-value: 2.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  115 QMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLG 194
Cdd:TIGR01349 278 EVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLG 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  195 MFGIDEFTAVINPPQACILAVG--RFRPVLKLTEDEegnaKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIR 272
Cdd:TIGR01349 358 MFGIKDFTAIINPPQACILAVGavEDVAVVDNDEEK----GFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIE 433


                  .
gi 260898739  273 L 273
Cdd:TIGR01349 434 M 434
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 56-114 1.09e-25

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.00  E-value: 1.09e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:PRK11892   2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKIL 60
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-114 8.73e-25

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.01  E-value: 8.73e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 260898739  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKIL 58
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-114 5.16e-24

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: 100.25  E-value: 5.16e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260898739   58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKIL 57
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-114 2.37e-22

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: 87.81  E-value: 2.37e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:COG0508    2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEIL 60
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 59-115 3.84e-13

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: 63.00  E-value: 3.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260898739   59 ILMPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVQ 115
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILV 58
 
Name Accession Description Interval E-value
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 109-273 6.07e-65

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: 202.00  E-value: 6.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  109 ILAKIV-----QMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPE 181
Cdd:pfam00198  45 FLVKAValalkKFPELNASWDGEEGEivYKKYVNIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  182 EYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEegnakLQQRQLITVTMSSDSRVVDDELATRFLK 261
Cdd:pfam00198 125 DLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGRIRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLN 199

                         170
                  ....*....|..
gi 260898739  262 SFKANLENPIRL 273
Cdd:pfam00198 200 TLKELLENPELL 211
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-273 1.83e-63

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 204.64  E-value: 1.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDG--------------------------- 108
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGtvakllveegdvvpvgsviavieeege 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739     --------------------------------------------------------------------------------
Cdd:PRK11856  82 aeaaaaaeaapeapapepapaaaaaaaaapaaaaapaapaaaaakaspavrklarelgvdlstvkgsgpggritkedvea 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739     --------------------------------------------------------------------------------
Cdd:PRK11856 162 aaaaaapaaaaaaaaaaappaaaaegeervplsgmrkaiakrmveskreiphftltdevdvtallalrkqlkaigvkltv 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 109 --ILAKIV-----QMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPE 181
Cdd:PRK11856 242 tdFLIKAValalkKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 182 EYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRF 259
Cdd:PRK11856 322 ELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGADAARF 394

                        410
                 ....*....|....
gi 260898739 260 LKSFKANLENPIRL 273
Cdd:PRK11856 395 LKALKELLENPALL 408
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 115-273 2.97e-59

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: 194.24  E-value: 2.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  115 QMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLG 194
Cdd:TIGR01349 278 EVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLG 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  195 MFGIDEFTAVINPPQACILAVG--RFRPVLKLTEDEegnaKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIR 272
Cdd:TIGR01349 358 MFGIKDFTAIINPPQACILAVGavEDVAVVDNDEEK----GFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIE 433


                  .
gi 260898739  273 L 273
Cdd:TIGR01349 434 M 434
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 115-270 5.29e-44

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 156.17  E-value: 5.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 115 QMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNL- 193
Cdd:PLN02744 381 KVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLg 460

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739 194 GMFGIDEFTAVINPPQACILAVGRF--RPVLKLTEDEEGNAklqqrQLITVTMSSDSRVVDDELATRFLKSFKANLENP 270
Cdd:PLN02744 461 GPFGIKQFCAIINPPQSAILAVGSAekRVIPGSGPDQYNFA-----SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 115-274 2.72e-36

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 135.34  E-value: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 115 QMPDVNVSWDGEGpKQLPF---IDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSIS 191
Cdd:PRK11855 390 EFPVFNASLDEDG-DELTYkkyFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTIS 468

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 192 NLGMFGIDEFTAVINPPQACILAVGRF--RPVlklTEDEEgnakLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLEN 269
Cdd:PRK11855 469 SLGGIGGTAFTPIINAPEVAILGVGKSqmKPV---WDGKE----FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLAD 541


                 ....*
gi 260898739 270 PIRLA 274
Cdd:PRK11855 542 PRRML 546
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 117-274 8.88e-36

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: 131.78  E-value: 8.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  117 PDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMF 196
Cdd:TIGR01347 248 PEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVF 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  197 GIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA 274
Cdd:TIGR01347 328 GSLMSTPIINPPQSAILGMHGIkeRPVAV-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 113-273 9.02e-34

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 128.97  E-value: 9.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 113 IVQMPDVNVSWDGEGpKQL---PFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFS 189
Cdd:PRK11854 474 LEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFT 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 190 ISNLGMFGIDEFTAVINPPQACILAVGR--FRPVlkltedeEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANL 267
Cdd:PRK11854 553 ISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV-------WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRL 625


                 ....*.
gi 260898739 268 ENPIRL 273
Cdd:PRK11854 626 SDIRRL 631
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 109-273 1.15e-32

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: 125.37  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  109 ILAKIV-----QMPDVNVSWDgEGPKQL---PFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLP 180
Cdd:TIGR01348 378 ILMKAVaaalkKFPKFNASLD-LGGEQLilkKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTP 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  181 EEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVLKLTEdeegnakLQQRQLITVTMSSDSRVVDDELATR 258
Cdd:TIGR01348 457 DEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPVWNGKE-------FEPRLMLPLSLSYDHRVIDGADAAR 529

                         170
                  ....*....|....*
gi 260898739  259 FLKSFKANLENPIRL 273
Cdd:TIGR01348 530 FTTYICESLADIRRL 544
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
117-273 6.44e-32

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 121.48  E-value: 6.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 117 PDVNVSWDGEGP--KQlpFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLG 194
Cdd:PRK05704 252 PEVNASIDGDDIvyHN--YYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 195 MFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIR 272
Cdd:PRK05704 330 VFGSLMSTPIINPPQSAILGMHKIkeRPVAV-------NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPER 402


                 .
gi 260898739 273 L 273
Cdd:PRK05704 403 L 403
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 95-273 1.15e-29

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 114.23  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  95 TDKAVVTLDASDDGILAKIVQMPDVNVSWDGEGPKQLP--FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKK 172
Cdd:PRK14843 170 TGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIIThnYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGR 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 173 ARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRV 250
Cdd:PRK14843 250 TLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRV 322

                        170       180
                 ....*....|....*....|...
gi 260898739 251 VDDELATRFLKSFKANLENPIRL 273
Cdd:PRK14843 323 VDGMAGAKFMKDLKELIETPISM 345
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 115-273 3.09e-29

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 114.39  E-value: 3.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 115 QMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLG 194
Cdd:PTZ00144 261 KMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGG 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 195 MFGIDEFTAVINPPQACIL---AVGRfRPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPI 271
Cdd:PTZ00144 341 VFGSLMGTPIINPPQSAILgmhAIKK-RPVVV-------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPA 412


                 ..
gi 260898739 272 RL 273
Cdd:PTZ00144 413 RM 414
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 56-114 1.09e-25

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 105.00  E-value: 1.09e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:PRK11892   2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKIL 60
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 117-273 7.22e-25

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 102.91  E-value: 7.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 117 PDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMF 196
Cdd:PLN02226 308 PVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVY 387

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739 197 GIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 273
Cdd:PLN02226 388 GSLISTPIINPPQSAILGMHSIvsRPMVV-------GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-114 8.73e-25

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.01  E-value: 8.73e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 260898739  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKIL 58
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-114 5.16e-24

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: 100.25  E-value: 5.16e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260898739   58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKIL 57
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 135-273 8.20e-23

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 96.71  E-value: 8.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 135 DISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 214
Cdd:PLN02528 277 NIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIA 356

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 215 VGRFRPVLKLTEDEE-GNAKlqqrqLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 273
Cdd:PLN02528 357 LGRIQKVPRFVDDGNvYPAS-----IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-114 2.37e-22

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: 87.81  E-value: 2.37e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:COG0508    2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEIL 60
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 134-270 4.35e-18

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 82.15  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739 134 IDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL 213
Cdd:PRK11857 169 LNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIA 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260898739 214 AVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENP 270
Cdd:PRK11857 249 GVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-114 5.73e-15

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 73.82  E-value: 5.73e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260898739  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:PRK14875   4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQV 60
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 59-113 2.59e-14

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: 66.31  E-value: 2.59e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 260898739  59 ILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKI 113
Cdd:cd06663    2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKV 56
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 59-115 3.84e-13

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: 63.00  E-value: 3.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260898739   59 ILMPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVQ 115
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILV 58
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 113-261 1.06e-07

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 52.59  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  113 IVQMPDVNVSWDGEGPKqlPFI----DISVAVATD-------KGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPE 181
Cdd:PRK12270  184 LKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTAD 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739  182 EYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFR-PVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFL 260
Cdd:PRK12270  262 DFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEyPAEFQGASEERLAELGISKVMTLTSTYDHRIIQGAESGEFL 341


                  .
gi 260898739  261 K 261
Cdd:PRK12270  342 R 342
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 71-122 4.70e-07

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


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 46.26  E-value: 4.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 260898739  71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVQMPDVNVS 122
Cdd:cd06850    8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVE 59
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 70-114 5.32e-07

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 50.21  E-value: 5.32e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 260898739  70 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIV 114
Cdd:PRK11855  15 EVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIK 59
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 57-126 1.37e-06

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: 49.24  E-value: 1.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260898739   57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVQMPDVNVSWDGE 126
Cdd:TIGR02927   3 ESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGV 72
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 54-126 7.95e-05

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: 43.85  E-value: 7.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260898739   54 GDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVQMPDVNVSWDGE 126
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTV 196
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 57-113 2.99e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.91  E-value: 2.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260898739  57 IKILMPSLSPTmeEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKI 113
Cdd:PRK11854   3 IEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEI 57
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 69-132 6.82e-04

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: 40.63  E-value: 6.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260898739   69 EEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKI-------VQMPDVNVSWDGEGPKQLP 132
Cdd:TIGR01348  12 EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIkvkvgdtLPVGGVIATLEVGAGAQAQ 82
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH