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Conserved domains on  [gi|1552104936|gb|AZZ50306|]
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2-oxo acid dehydrogenase subunit E2 [Rathayibacter rathayi]

Protein Classification

dihydrolipoamide acetyltransferase family protein( domain architecture ID 11485570)

dihydrolipoamide acetyltransferase family protein is the acetyltransferase (E2) subunit of a 2-oxo acid dehydrogenase multienzyme complex, such as Pseudomonas putida lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex

EC:  2.3.-.-
Gene Ontology:  GO:0016407|GO:0045240
PubMed:  3332999|24077172
SCOP:  4000430

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-441 2.00e-158

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


:

Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 453.86  E-value: 2.00e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   1 MTEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGA 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  81 GvigsevPAIPAHPSQAATAPAPSTTepgegsgaalvgygtaggqvqtrrrrsgPTAAPTRPTAPARPASVPAAAALPVI 160
Cdd:PRK11856   81 E------AEAAAAAEAAPEAPAPEPA----------------------------PAAAAAAAAAPAAAAAPAAPAAAAAK 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 161 AKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRNIQTPAWS------DDREERVPVRGVRKAIAAAMST 234
Cdd:PRK11856  127 ASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAappaaaAEGEERVPLSGMRKAIAKRMVE 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 235 SAFTAPHVSVFVDVDATRTMEFVKRLKNspdfAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAAT 314
Cdd:PRK11856  207 SKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVAT 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 315 PRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKP 394
Cdd:PRK11856  283 DGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERP 362

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1552104936 395 WVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PRK11856  363 VVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
 
Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-441 2.00e-158

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 453.86  E-value: 2.00e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   1 MTEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGA 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  81 GvigsevPAIPAHPSQAATAPAPSTTepgegsgaalvgygtaggqvqtrrrrsgPTAAPTRPTAPARPASVPAAAALPVI 160
Cdd:PRK11856   81 E------AEAAAAAEAAPEAPAPEPA----------------------------PAAAAAAAAAPAAAAAPAAPAAAAAK 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 161 AKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRNIQTPAWS------DDREERVPVRGVRKAIAAAMST 234
Cdd:PRK11856  127 ASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAappaaaAEGEERVPLSGMRKAIAKRMVE 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 235 SAFTAPHVSVFVDVDATRTMEFVKRLKNspdfAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAAT 314
Cdd:PRK11856  207 SKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVAT 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 315 PRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKP 394
Cdd:PRK11856  283 DGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERP 362

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1552104936 395 WVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PRK11856  363 VVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 232-441 7.15e-85

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: 258.63  E-value: 7.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 232 MSTSAFTAPHVSVFVDVDATRTMEFVKRLKNSPDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTD--SEIIVRHYVNLG 309
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGeeGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 310 IAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGT 389
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1552104936 390 IKQKPWVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 6-442 9.66e-80

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: 252.35  E-value: 9.66e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   6 LLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGAGVigs 85
Cdd:TIGR01347   4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  86 evpaiPAHPSQAATAPAPsttepgegsgaalvgygtaggqvqtrrrrsgptaaptrPTAPARPASVPAAAALPVIAKPPI 165
Cdd:TIGR01347  81 -----TAAPPAKSGEEKE--------------------------------------ETPAASAAAAPTAAANRPSLSPAA 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 166 RKLAKDLDVDLVEVQATGLAGEVTRDDVIRH------ASQASVFRNIQTPAWSDDREERVPVRGVRKAIAAAMSTSAFTA 239
Cdd:TIGR01347 118 RRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKteapasAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNST 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 240 PHVSVFVDVDATRTMEFVKRLKNspDFA---GVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAATPR 316
Cdd:TIGR01347 198 AMLTTFNEVDMSAVMELRKRYKE--EFEkkhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDR 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 317 GLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKPWV 396
Cdd:TIGR01347 276 GLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVA 355

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1552104936 397 VDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPA-LLLD 442
Cdd:TIGR01347 356 VNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRrLLLD 402
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-76 2.01e-27

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: 103.99  E-value: 2.01e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552104936   1 MTEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:COG0508     1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 4-76 7.91e-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: 97.09  E-value: 7.91e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552104936   4 QFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-441 2.00e-158

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 453.86  E-value: 2.00e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   1 MTEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGA 80
Cdd:PRK11856    1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  81 GvigsevPAIPAHPSQAATAPAPSTTepgegsgaalvgygtaggqvqtrrrrsgPTAAPTRPTAPARPASVPAAAALPVI 160
Cdd:PRK11856   81 E------AEAAAAAEAAPEAPAPEPA----------------------------PAAAAAAAAAPAAAAAPAAPAAAAAK 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 161 AKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRNIQTPAWS------DDREERVPVRGVRKAIAAAMST 234
Cdd:PRK11856  127 ASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAappaaaAEGEERVPLSGMRKAIAKRMVE 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 235 SAFTAPHVSVFVDVDATRTMEFVKRLKNspdfAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAAT 314
Cdd:PRK11856  207 SKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVAT 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 315 PRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKP 394
Cdd:PRK11856  283 DGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERP 362

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1552104936 395 WVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PRK11856  363 VVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 2-442 5.69e-108

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 329.86  E-value: 5.69e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   2 TEQFLLPDVGEgLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIItvrsgag 81
Cdd:PRK11855  119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLV------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  82 VIGSEVPAIPAHPSQAATAPAPSTTepgegsgaalvgygtaggqvqtrrrrsgPTAAPTRPTAPARPASVPAAAALP--- 158
Cdd:PRK11855  191 VIEVAAAAPAAAAAPAAAAPAAAAA----------------------------AAPAPAPAAAAAPAAAAPAAAAAPgka 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 159 VIAKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRNIQTPA-------------W-----SDDRE-ERV 219
Cdd:PRK11855  243 PHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAaaaagggglgllpWpkvdfSKFGEiETK 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 220 PVRGVRKAIAAAMSTSAFTAPHVSVFVDVDATRTMEFVKRLKNSPDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDS- 298
Cdd:PRK11855  323 PLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDg 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 299 -EIIVRHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPIL 377
Cdd:PRK11855  403 dELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPII 482

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552104936 378 NPGEVAIIALGTIKQKPWVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLLD 442
Cdd:PRK11855  483 NAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 232-441 7.15e-85

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: 258.63  E-value: 7.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 232 MSTSAFTAPHVSVFVDVDATRTMEFVKRLKNSPDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTD--SEIIVRHYVNLG 309
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGeeGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 310 IAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGT 389
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1552104936 390 IKQKPWVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 6-442 9.66e-80

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: 252.35  E-value: 9.66e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   6 LLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGAGVigs 85
Cdd:TIGR01347   4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  86 evpaiPAHPSQAATAPAPsttepgegsgaalvgygtaggqvqtrrrrsgptaaptrPTAPARPASVPAAAALPVIAKPPI 165
Cdd:TIGR01347  81 -----TAAPPAKSGEEKE--------------------------------------ETPAASAAAAPTAAANRPSLSPAA 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 166 RKLAKDLDVDLVEVQATGLAGEVTRDDVIRH------ASQASVFRNIQTPAWSDDREERVPVRGVRKAIAAAMSTSAFTA 239
Cdd:TIGR01347 118 RRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKteapasAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNST 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 240 PHVSVFVDVDATRTMEFVKRLKNspDFA---GVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAATPR 316
Cdd:TIGR01347 198 AMLTTFNEVDMSAVMELRKRYKE--EFEkkhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDR 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 317 GLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKPWV 396
Cdd:TIGR01347 276 GLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVA 355

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1552104936 397 VDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPA-LLLD 442
Cdd:TIGR01347 356 VNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRrLLLD 402
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-442 6.88e-77

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 245.13  E-value: 6.88e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   1 MTEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGA 80
Cdd:PRK05704    1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  81 gvigsevpaipahpsqAATAPAPSttepgegsgaalvgygtaggqvqtrrrrsgPTAAPTRPTAPARPASVPAAAALPVI 160
Cdd:PRK05704   81 ----------------AAGAAAAA------------------------------AAAAAAAAAAPAQAQAAAAAEQSNDA 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 161 AKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRN-------IQTPAWSDDR-EERVPVRGVRKAIA--- 229
Cdd:PRK05704  115 LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAapaaaapAAAPAPLGARpEERVPMTRLRKTIAerl 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 230 ------AAMSTSaftaphvsvFVDVDATRTMEFVKRLKNSpdFA---GVKvspLLIMA---KAIIWAVRRNPTVNSAWTD 297
Cdd:PRK05704  195 leaqntTAMLTT---------FNEVDMTPVMDLRKQYKDA--FEkkhGVK---LGFMSffvKAVVEALKRYPEVNASIDG 260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 298 SEIIVRHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPIL 377
Cdd:PRK05704  261 DDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPII 340

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552104936 378 NPGEVAIIALGTIKQKPWVVDGEVRPRFVTTVGGSFDHRVVDG-DVVSrFVADVASVLEEPA-LLLD 442
Cdd:PRK05704  341 NPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGkEAVG-FLVTIKELLEDPErLLLD 406
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 8-435 4.08e-76

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 249.53  E-value: 4.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   8 PDVGegLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVrsgaGVIGSEV 87
Cdd:PRK11854  212 PDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF----EVEGAAP 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  88 PAIPAHPSQAATAPAPSTTEPgegsgaalvgygtaggqvqtrrrrsgPTAAPtrPTAPARPASVPAAAALPViAKPPIRK 167
Cdd:PRK11854  286 AAAPAKQEAAAPAPAAAKAEA--------------------------PAAAP--AAKAEGKSEFAENDAYVH-ATPLVRR 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 168 LAKDLDVDLVEVQATGLAGEVTRDDVIRHASQAsVFRNIQTPAWS--------------------DDREErVPVRGVRKA 227
Cdd:PRK11854  337 LAREFGVNLAKVKGTGRKGRILKEDVQAYVKDA-VKRAEAAPAAAaaggggpgllpwpkvdfskfGEIEE-VELGRIQKI 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 228 IAAAMSTSAFTAPHVSVFVDVDATRTMEFVKRlKNSPDFA---GVKVSPLLIMAKAIIWAVRRNPTVNSAWTDS--EIIV 302
Cdd:PRK11854  415 SGANLHRNWVMIPHVTQFDKADITELEAFRKQ-QNAEAEKrklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDgqRLTL 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 303 RHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEV 382
Cdd:PRK11854  494 KKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEV 573

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1552104936 383 AIIALGTIKQKPwVVDG-EVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLE 435
Cdd:PRK11854  574 AILGVSKSAMEP-VWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 5-441 4.51e-70

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 227.68  E-value: 4.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   5 FLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAI--ITVRSGAGV 82
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLlkIMVEDSQHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  83 IGSevpaipahpsqaatapapSTTEPGEGSGAALVGYGTAGGQVQtrrrrSGptaaptrptaparpasvpaaaalpVIAK 162
Cdd:PLN02528   81 RSD------------------SLLLPTDSSNIVSLAESDERGSNL-----SG------------------------VLST 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 163 PPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASV------------------FRNIQTPAWSDDREERVPVRGV 224
Cdd:PLN02528  114 PAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVvkdsssaeeatiaeqeefSTSVSTPTEQSYEDKTIPLRGF 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 225 RKAIAAAMsTSAFTAPHVsVFVD---VDATrtMEFVKRLKNSPDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTD--SE 299
Cdd:PLN02528  194 QRAMVKTM-TAAAKVPHF-HYVEeinVDAL--VELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEetSE 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 300 IIVRHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNP 379
Cdd:PLN02528  270 IRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNL 349

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552104936 380 GEVAIIALGTIKQKPWVVD-GEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PLN02528  350 PEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 3-441 1.77e-69

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: 229.76  E-value: 1.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   3 EQFLLPDVGeGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGAGV 82
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGST 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  83 IGSEV---PAIPAHPSQAATAPAPSttepgegsgaalvgygtaggqvqtrrrrSGPTAAPTRPTAPARPASVPAAAALPv 159
Cdd:TIGR01348 196 PATAPapaSAQPAAQSPAATQPEPA----------------------------AAPAAAKAQAPAPQQAGTQNPAKVDH- 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 160 iAKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVfrniQTPAWSDDRE--------------------ERV 219
Cdd:TIGR01348 247 -AAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSV----RAQAAAASAAggapgalpwpnvdfskfgevEEV 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 220 PVRGVRKAIAAAMSTSAFTAPHVSVFVDVDATRTMEFVKRLKNSPDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDS- 298
Cdd:TIGR01348 322 DMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGg 401

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 299 -EIIVRHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPIL 377
Cdd:TIGR01348 402 eQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIV 481

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552104936 378 NPGEVAIIALGTIKQKPwVVDG-EVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:TIGR01348 482 NAPEVAILGVSKSGMEP-VWNGkEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 7-441 5.71e-69

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 224.95  E-value: 5.71e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   7 LPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGagvigse 86
Cdd:PTZ00144   49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTG------- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  87 vPAIPAHPSQAATAPAPSTTEPGEgsgaalvgygtaggqvqtrrrrsgPTAAPTRPTAPARPASVPAAAALPVIAKPPIR 166
Cdd:PTZ00144  122 -GAPPAAAPAAAAAAKAEKTTPEK------------------------PKAAAPTPEPPAASKPTPPAAAKPPEPAPAAK 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 167 KLAKDLDVdlvevqatglagevtrddvirhasqasvfrniqtpawSDDREERVPVRGVRKAIAAAMSTSAFTAPHVSVFV 246
Cdd:PTZ00144  177 PPPTPVAR-------------------------------------ADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFN 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 247 DVDATRTMEFVKRLKnsPDFA---GVK---VSPLLimaKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAATPRGLLV 320
Cdd:PTZ00144  220 ECDMSALMELRKEYK--DDFQkkhGVKlgfMSAFV---KASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 321 PNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKPWVVDGE 400
Cdd:PTZ00144  295 PVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE 374

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1552104936 401 VRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PTZ00144  375 IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 6-436 2.44e-60

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: 206.40  E-value: 2.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   6 LLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIitVRSGAGVIGS 85
Cdd:TIGR02927 130 KMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVL--AIIGDANAAP 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  86 EVPAIPAHPSQAATAPAPSTTEPGEGSGAAlvgygtaggqvqtrRRRSGPTAAPTRPTAPARPASVPAAAALPVIAkPPI 165
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEPAPDPAARAPHAA--------------PDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVT-PLV 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 166 RKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRNIQT-------------------PAWSDDREERVPVRGVRK 226
Cdd:TIGR02927 273 RKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAapaaaaapaapaaaakpaePDTAKLRGTTQKMNRIRQ 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 227 AIAAAMSTSAFTAPHVSVFVDVDATRTMEFvkRLKNSPDFA---GVKVSPLLIMAKAIIWAVRRNPTVNSAWTD--SEII 301
Cdd:TIGR02927 353 ITADKTIESLQTSAQLTQVHEVDMTRVAAL--RARAKNDFLeknGVNLTFLPFFVQAVTEALKAHPNVNASYNAetKEVT 430

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 302 VRHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGE 381
Cdd:TIGR02927 431 YHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQ 510

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 382 VAIIALGTIKQKPWVVDGE-----VRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEE 436
Cdd:TIGR02927 511 AAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 2-442 1.94e-50

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 177.25  E-value: 1.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   2 TEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVRSGAG 81
Cdd:PLN02226   91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  82 VIGSEVPAIPAhPSQAATAPAPsttePGEGSgaalvgygtaggqvQTRRRRSGPTAAptRPTAPARPasvpaaaalpvia 161
Cdd:PLN02226  171 AASQVTPSQKI-PETTDPKPSP----PAEDK--------------QKPKVESAPVAE--KPKAPSSP------------- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 162 kPPIRKLAKDldvdlvevqatglagevtrddvirhasqasvfrnIQTPAwsDDREERVPVRGVRKAIAAAMSTSAFTAPH 241
Cdd:PLN02226  217 -PPPKQSAKE----------------------------------PQLPP--KERERRVPMTRLRKRVATRLKDSQNTFAL 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 242 VSVFVDVDATRTMEFVKRLKNS-PDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSEIIVRHYVNLGIAAATPRGLLV 320
Cdd:PLN02226  260 LTTFNEVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVV 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 321 PNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIKQKPWVVDGE 400
Cdd:PLN02226  340 PVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGS 419

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1552104936 401 VRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPA-LLLD 442
Cdd:PLN02226  420 VVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQrLLLD 462
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 7-441 2.38e-49

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 176.20  E-value: 2.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   7 LPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEG-QTVDVGTAI-ITV--RSGAGV 82
Cdd:PLN02744  117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIaITVeeEEDIGK 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  83 IGSEVPAIPAHPsqAATAPAPSTTEPGEgsgaalvgygtaggqvqTRRRRSGPTaaptrPTAPARPASVPAAAALPVIAK 162
Cdd:PLN02744  197 FKDYKPSSSAAP--AAPKAKPSPPPPKE-----------------EEVEKPASS-----PEPKASKPSAPPSSGDRIFAS 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 163 PPIRKLAKDLDVDLVEVQATGLAGEVTRDDV----IRHASQASVFRNIQTPAWSDDREErVPVRGVRKAIAAAMSTSAFT 238
Cdd:PLN02744  253 PLARKLAEDNNVPLSSIKGTGPDGRIVKADIedylASGGKGATAPPSTDSKAPALDYTD-IPNTQIRKVTASRLLQSKQT 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 239 APHVSVFVDVDATRTMEFVKRLKNSPDFAGVK---VSPLLIMAKAIiwAVRRNPTVNSAWTDSEIIVRHYVNLGIAAATP 315
Cdd:PLN02744  332 IPHYYLTVDTRVDKLMALRSQLNSLQEASGGKkisVNDLVIKAAAL--ALRKVPQCNSSWTDDYIRQYHNVNINVAVQTE 409

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 316 RGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNI-GVFGMDTGTPILNPGEVAIIALGTIKQK- 393
Cdd:PLN02744  410 NGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRv 489

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1552104936 394 -PWVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PLN02744  490 iPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 163-441 9.86e-48

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 167.00  E-value: 9.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 163 PPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRHASQASVFRNIQTPAWSDDRE------------ERVPVRGVRKAIAA 230
Cdd:PRK14843   53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEevpdnvtpygeiERIPMTPMRKVIAQ 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 231 AMSTSAFTAPHVSVFVDVDATRTMEFVKR-LKNSPDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTD--SEIIVRHYVN 307
Cdd:PRK14843  133 RMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEdgKTIITHNYVN 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 308 LGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIAL 387
Cdd:PRK14843  213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1552104936 388 GTIKQKPWVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALLL 441
Cdd:PRK14843  293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 159-440 9.27e-46

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 160.73  E-value: 9.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 159 VIAKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDVIRH----------ASQASVFRNIQTPAWSDDRE-------ERVPV 221
Cdd:PRK11857    2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFikslksaptpAEAASVSSAQQAAKTAAPAAappklegKREKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 222 RGVRKAIAAAMSTSAFTAPHVSVFVDVDATRTMEFVKRLKNS-PDFAGVKVSPLLIMAKAIIWAVRRNPTVNSAWTD--S 298
Cdd:PRK11857   82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEatS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 299 EIIVRHYVNLGIAAATPRGLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILN 378
Cdd:PRK11857  162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552104936 379 PGEVAIIALGTIKQKPWVVDGEVRPRFVTTVGGSFDHRVVDGDVVSRFVADVASVLEEPALL 440
Cdd:PRK11857  242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-76 2.01e-27

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: 103.99  E-value: 2.01e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552104936   1 MTEQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:COG0508     1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 4-76 7.91e-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: 97.09  E-value: 7.91e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552104936   4 QFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 93-420 2.13e-22

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 100.35  E-value: 2.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   93 HPSQAATAPAPSTTEPGEGSGAALVGYGTAGGQVQTrrrrsgPTAAPTRPTAPARPASVPAAAALPVIAKPPIRKLAkdl 172
Cdd:PRK12270    37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAP------APPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAA--- 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  173 dvdlvevqatglagevtrddvirhasqasvfrniqtPAWSDDREERVPVRGVRKAIAAAMSTSaFTAPHVSVFVDVDAT- 251
Cdd:PRK12270   108 ------------------------------------PAAAAVEDEVTPLRGAAAAVAKNMDAS-LEVPTATSVRAVPAKl 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  252 ----RTM--EFVKRLKnspdfaGVKVSPLLIMAKAIIWAVRRNPTVNSAWTDSE----IIVRHYVNLGIAAATP-----R 316
Cdd:PRK12270   151 lidnRIVinNHLKRTR------GGKVSFTHLIGYALVQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAIDLPkkdgsR 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  317 GLLVPNVKDAQSMSLLELAQALEKLTLDARDGKTTAADMQNGTITITNIGVFGMDTGTPILNPGEVAIIALGTIkqkpwv 396
Cdd:PRK12270   225 QLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM------ 298

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1552104936  397 vdgEVRPRF---------------VTTVGGSFDHRVVDG 420
Cdd:PRK12270   299 ---EYPAEFqgaseerlaelgiskVMTLTSTYDHRIIQG 334
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 3-76 8.27e-18

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: 77.64  E-value: 8.27e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552104936   3 EQFLLPDVGEGLTEAeIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:pfam00364   1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-120 1.66e-12

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 68.43  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   6 LLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGtAIITVRSGAGVIGS 85
Cdd:PRK14875    6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVG-ALLAVVADAEVSDA 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1552104936  86 EV---------PAIPAHPSQAATAPAPSTTE----------PGEGSGAALV---GYG 120
Cdd:PRK14875   85 EIdafiapfarRFAPEGIDEEDAGPAPRKARiggrtvrylrLGEGDGTPVVlihGFG 141
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 19-76 5.16e-12

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: 60.89  E-value: 5.16e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1552104936  19 IVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:cd06850    10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 4-74 2.61e-11

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: 58.99  E-value: 2.61e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552104936   4 QFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAII 74
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 24-77 8.39e-10

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 56.83  E-value: 8.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1552104936  24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVR 77
Cdd:COG0511    83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 19-77 6.21e-08

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 54.85  E-value: 6.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1552104936  19 IVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITVR 77
Cdd:PRK09282  533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 159-193 5.90e-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: 45.76  E-value: 5.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1552104936 159 VIAKPPIRKLAKDLDVDLVEVQATGLAGEVTRDDV 193
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 8-74 1.77e-06

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 47.55  E-value: 1.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552104936   8 PDVGEGLTEA----EIVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAII 74
Cdd:PRK05641   80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
GcvH COG0509
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ...
 25-67 4.49e-06

Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440275  Cd Length: 128  Bit Score: 45.88  E-value: 4.49e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1552104936  25 KVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDV---LVDEGQTV 67
Cdd:COG0509    46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEVneaLEDDPELV 91
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 24-70 6.14e-06

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 48.92  E-value: 6.14e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1552104936   24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVG 70
Cdd:COG1038   1092 VKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 25-59 7.78e-06

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 44.06  E-value: 7.78e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1552104936  25 KVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDV 59
Cdd:cd06848    38 EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV 72
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
24-76 3.03e-05

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 46.46  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1552104936  24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:PRK14040  540 VTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 24-71 9.37e-05

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 44.06  E-value: 9.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1552104936  24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGT 71
Cdd:PLN02983  220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDT 267
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
24-76 1.41e-04

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 40.38  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1552104936  24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:PRK07051   26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 24-70 3.58e-04

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 43.20  E-value: 3.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1552104936   24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVG 70
Cdd:PRK12999  1092 VKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG 1138
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 24-76 4.69e-04

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 40.18  E-value: 4.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1552104936  24 VKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:PRK06549   77 VAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 19-76 5.66e-04

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 42.40  E-value: 5.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1552104936  19 IVAWRVKVGDEVAVNQVLVEIETAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:PRK14042  536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
PHA02030 PHA02030
hypothetical protein
 52-157 1.11e-03

hypothetical protein


Pssm-ID: 222843 [Multi-domain]  Cd Length: 336  Bit Score: 41.12  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  52 FSGTVVDVLVDegqtvdvGTAIITVRSGAGVIGSEVPAIPAHPSQAATAPAPSTTEPGEGSGAALVGY-GTAGGQVQTRR 130
Cdd:PHA02030  238 FPGSALHILLG-------GGEDLIIKPKSKAAGSNLPAVPNVAADAGSAAAPAVPAAAAAVAQAAPSVpQVPNVAVLPDV 310

                          90       100
                  ....*....|....*....|....*..
gi 1552104936 131 RRSGPTAAPTRPTAPARPAsVPAAAAL 157
Cdd:PHA02030  311 PQVAPVAAPAAPEVPAVPV-VPAAPQV 336
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
80-165 2.68e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  80 AGVIGSEVPAIPAHPSQAATAPAPSTTEP---GEGSGAALVGYGTAGGQVQTRRRRsgptaaptRPTAPARPASVPAAAA 156
Cdd:PRK07003  514 AAASREDAPAAAAPPAPEARPPTPAAAAPaarAGGAAAALDVLRNAGMRVSSDRGA--------RAAAAAKPAAAPAAAP 585


                  ....*....
gi 1552104936 157 LPVIAKPPI 165
Cdd:PRK07003  586 KPAAPRVAV 594
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
88-243 2.90e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  88 PAIPAHPSQAATAPAPSTTEPGEGSGAALVGYGTAGGQVQTRRRRSGPTAAP-------TRPTAPARPASVPAAAALPVI 160
Cdd:PRK12323  403 PAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPaaapaaaARPAAAGPRPVAAAAAAAPAR 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936 161 AKPPIRKLAKDLDVDLVEVQATGLAgeVTRDDVIRHASQASVFRNIQTPAWSDDREERvPVRGVRKAIAAAMSTSAFTAP 240
Cdd:PRK12323  483 AAPAAAPAPADDDPPPWEELPPEFA--SPAPAQPDAAPAGWVAESIPDPATADPDDAF-ETLAPAPAAAPAPRAAAATEP 559


                  ...
gi 1552104936 241 HVS 243
Cdd:PRK12323  560 VVA 562
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
64-164 5.55e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.09  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936  64 GQTVDVGTAIITVRSGAGVIGSEVPAIPA-HPSQAATAPAPSTTEPGEGSGAALVGYGTAGGQVQTRRRRSGPTAAPTRP 142
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPApAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449

                          90       100
                  ....*....|....*....|..
gi 1552104936 143 TAPArPASVPAAAALPVIAKPP 164
Cdd:PRK12323  450 PAPA-PAAAPAAAARPAAAGPR 470
PHA03247 PHA03247
large tegument protein UL36; Provisional
 85-164 5.95e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 5.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552104936   85 SEVPAIPAHPSQAATAPAPSTTEPGEGSGAALV-----GYGTAGGQVQTRRRRS------GPTAAPTRPTAPARPASVPA 153
Cdd:PHA03247  2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPpperpRDDPAPGRVSRPRRARrlgraaQASSPPQRPRRRAARPTVGS 2694

                           90
                   ....*....|.
gi 1552104936  154 AAALpviAKPP 164
Cdd:PHA03247  2695 LTSL---ADPP 2702
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 3-76 7.09e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 38.67  E-value: 7.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552104936   3 EQFLLPDVGEGLTEAEIVAWRVKVGDEVAVNQVLVEIE-----TAKSLVELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:PRK09282  475 EKYEVKIEGVKAEGKRPFYLRVDGMPEEVVVEPLKEIVvggrpRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVL 553
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 47-76 9.26e-03

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: 34.70  E-value: 9.26e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1552104936  47 ELPSPFSGTVVDVLVDEGQTVDVGTAIITV 76
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVL 30
 
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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