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Conserved domains on  [gi|954047865|gb|ALP41623|]
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pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase component [Aeromonas schubertii]

Protein Classification

dihydrolipoamide acetyltransferase family protein( domain architecture ID 11485570)

dihydrolipoamide acetyltransferase family protein, similar to dihydrolipoyllysine-residue acetyltransferase, the E2 subunit of the 2-oxo acid dehydrogenase complex, and to lipoamide acyltransferase, the E2 subunit of pyruvate dehydrogenase

EC:  2.3.1.-
Gene Ontology:  GO:0006096

Graphical summary

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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
 1-363 9.55e-123

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


:

Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 359.88  E-value: 9.55e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   1 MKFFKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGED 80
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  81 DGTAVGKVHGSSQVLEDHFVVGAVAAGGSLTQ-------------AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQ 147
Cdd:PRK11856  82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapaaaaakASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 148 AFEAQGGSHNEI-------------------LKGARRAMAKAMTLSHQSVVPVTITDEVD---LRAWRSDED-------V 198
Cdd:PRK11856 162 AAAAAAPAAAAAaaaaaappaaaaegeervpLSGMRKAIAKRMVESKREIPHFTLTDEVDvtaLLALRKQLKaigvkltV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 199 TVRLIRGIGVACRAEPSMNAWFDGETLTRrlFDEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVP 278
Cdd:PRK11856 242 TDFLIKAVALALKKFPELNASWDDDAIVL--KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 279 REMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALV 358
Cdd:PRK11856 320 PEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALK 399


                 ....*
gi 954047865 359 NALES 363
Cdd:PRK11856 400 ELLEN 404
 
Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-363 9.55e-123

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 359.88  E-value: 9.55e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   1 MKFFKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGED 80
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  81 DGTAVGKVHGSSQVLEDHFVVGAVAAGGSLTQ-------------AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQ 147
Cdd:PRK11856  82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapaaaaakASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 148 AFEAQGGSHNEI-------------------LKGARRAMAKAMTLSHQSVVPVTITDEVD---LRAWRSDED-------V 198
Cdd:PRK11856 162 AAAAAAPAAAAAaaaaaappaaaaegeervpLSGMRKAIAKRMVESKREIPHFTLTDEVDvtaLLALRKQLKaigvkltV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 199 TVRLIRGIGVACRAEPSMNAWFDGETLTRrlFDEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVP 278
Cdd:PRK11856 242 TDFLIKAVALALKKFPELNASWDDDAIVL--KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 279 REMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALV 358
Cdd:PRK11856 320 PEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALK 399


                 ....*
gi 954047865 359 NALES 363
Cdd:PRK11856 400 ELLEN 404
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 171-362 3.78e-54

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: 177.35  E-value: 3.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  171 MTLSHQSVVPVTITDEVD---LRAWR-------SDED----VTVRLIRGIGVACRAEPSMNAWFDGETLTRRLFDEVNVA 236
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDvteLLALReelkedaADEEtkltFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  237 IAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVPREMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGK 316
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 954047865  317 LFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALVNALE 362
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 5-362 3.61e-48

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: 167.60  E-value: 3.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865    5 KLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGEDDGTA 84
Cdd:TIGR01347   4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   85 VGKVHGSSQvlEDHFVVGAVAAGGSLTQ---AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQAFEA-----QGGSH 156
Cdd:TIGR01347  84 PPAKSGEEK--EETPAASAAAAPTAAANrpsLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEApasaqPPAAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  157 NEILKGA--------------RRAMAKAMTLSHQSVVPVTITDEVD------LRAWRSDE---DVTVRL------IRGIG 207
Cdd:TIGR01347 162 AAAAAPAaatrpeervkmtrlRQRIAERLKEAQNSTAMLTTFNEVDmsavmeLRKRYKEEfekKHGVKLgfmsffVKAVV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  208 VACRAEPSMNAWFDG-ETLTRRLFDevnVAIAVDSRHGLYVPVMENvVDRAGAdlrGGLDRMIAD--VKARA--VPREML 282
Cdd:TIGR01347 242 AALKRFPEVNAEIDGdDIVYKDYYD---ISVAVSTDRGLVVPVVRN-ADRMSF---ADIEKEIADlgKKARDgkLTLEDM 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  283 QGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNG--EARPVRALPLSvtFDHRACTGGEAARFLRALVNA 360
Cdd:TIGR01347 315 TGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGqiEIRPMMYLALS--YDHRLIDGKEAVTFLVTIKEL 392


                  ..
gi 954047865  361 LE 362
Cdd:TIGR01347 393 LE 394
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 4-75 1.27e-25

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: 98.22  E-value: 1.27e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 954047865   4 FKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:COG0508    5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 4-75 3.28e-24

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.39  E-value: 3.28e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 954047865   4 FKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:cd06849    3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-363 9.55e-123

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 359.88  E-value: 9.55e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   1 MKFFKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGED 80
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  81 DGTAVGKVHGSSQVLEDHFVVGAVAAGGSLTQ-------------AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQ 147
Cdd:PRK11856  82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapaaaaakASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 148 AFEAQGGSHNEI-------------------LKGARRAMAKAMTLSHQSVVPVTITDEVD---LRAWRSDED-------V 198
Cdd:PRK11856 162 AAAAAAPAAAAAaaaaaappaaaaegeervpLSGMRKAIAKRMVESKREIPHFTLTDEVDvtaLLALRKQLKaigvkltV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 199 TVRLIRGIGVACRAEPSMNAWFDGETLTRrlFDEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVP 278
Cdd:PRK11856 242 TDFLIKAVALALKKFPELNASWDDDAIVL--KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 279 REMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALV 358
Cdd:PRK11856 320 PEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALK 399


                 ....*
gi 954047865 359 NALES 363
Cdd:PRK11856 400 ELLEN 404
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 4-362 1.92e-68

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 224.32  E-value: 1.92e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   4 FKLPDLGEgLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGED--- 80
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAapa 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  81 ------------DGTAVGKVHGSSQVLEDHFVVGAVAAGGSLTQAMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQA 148
Cdd:PRK11855 201 aaaapaaaapaaAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAF 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 149 FE---------------AQGGSHN-----------------EILKGARRAMAKAMTLSHQSVVPVTITDEVD---LRAWR 193
Cdd:PRK11855 281 VKgamsaaaaaaaaaaaAGGGGLGllpwpkvdfskfgeietKPLSRIKKISAANLHRSWVTIPHVTQFDEADitdLEALR 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 194 -------SDEDVTVR----LIRGIGVACRAEPSMNAWFD--GETLTrrLFDEVNVAIAVDSRHGLYVPVMENVVDRAGAD 260
Cdd:PRK11855 361 kqlkkeaEKAGVKLTmlpfFIKAVVAALKEFPVFNASLDedGDELT--YKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLE 438

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 261 LRggldRMIADVKARA-----VPREMlQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGEARPVRALP 335
Cdd:PRK11855 439 IA----REIAELAKKArdgklKPDDM-QGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLP 513

                        410       420
                 ....*....|....*....|....*..
gi 954047865 336 LSVTFDHRACTGGEAARFLRALVNALE 362
Cdd:PRK11855 514 LSLSYDHRVIDGATAARFTNYLKQLLA 540
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 4-353 1.50e-56

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 189.93  E-value: 1.50e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   4 FKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGgEDDGT 83
Cdd:PLN02528   1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMV-EDSQH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  84 AVGKVHGSSQVLEDHFVVGAVAAGGSLT---QAMPAVRRLALQLGVDVEHLKGSGPAGLVTEADV--------------- 145
Cdd:PLN02528  80 LRSDSLLLPTDSSNIVSLAESDERGSNLsgvLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkyaaqkgvvkdsss 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 146 -QQAFEAQGGSHNEI---------------LKGARRAMAKAMTLSHQsvVP-VTITDE------VDLRAWRSDE--DVTV 200
Cdd:PLN02528 160 aEEATIAEQEEFSTSvstpteqsyedktipLRGFQRAMVKTMTAAAK--VPhFHYVEEinvdalVELKASFQENntDPTV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 201 R------LIRGIGVACRAEPSMNAWFDGETLTRRLFDEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKA 274
Cdd:PLN02528 238 KhtflpfLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 275 RAVPREMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVN-GEARPVRALPLSVTFDHRACTGGEAARF 353
Cdd:PLN02528 318 NKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARF 397
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 171-362 3.78e-54

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: 177.35  E-value: 3.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  171 MTLSHQSVVPVTITDEVD---LRAWR-------SDED----VTVRLIRGIGVACRAEPSMNAWFDGETLTRRLFDEVNVA 236
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDvteLLALReelkedaADEEtkltFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  237 IAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVPREMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGK 316
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 954047865  317 LFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALVNALE 362
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 5-362 3.61e-48

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: 167.60  E-value: 3.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865    5 KLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGEDDGTA 84
Cdd:TIGR01347   4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   85 VGKVHGSSQvlEDHFVVGAVAAGGSLTQ---AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQAFEA-----QGGSH 156
Cdd:TIGR01347  84 PPAKSGEEK--EETPAASAAAAPTAAANrpsLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEApasaqPPAAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  157 NEILKGA--------------RRAMAKAMTLSHQSVVPVTITDEVD------LRAWRSDE---DVTVRL------IRGIG 207
Cdd:TIGR01347 162 AAAAAPAaatrpeervkmtrlRQRIAERLKEAQNSTAMLTTFNEVDmsavmeLRKRYKEEfekKHGVKLgfmsffVKAVV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  208 VACRAEPSMNAWFDG-ETLTRRLFDevnVAIAVDSRHGLYVPVMENvVDRAGAdlrGGLDRMIAD--VKARA--VPREML 282
Cdd:TIGR01347 242 AALKRFPEVNAEIDGdDIVYKDYYD---ISVAVSTDRGLVVPVVRN-ADRMSF---ADIEKEIADlgKKARDgkLTLEDM 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  283 QGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNG--EARPVRALPLSvtFDHRACTGGEAARFLRALVNA 360
Cdd:TIGR01347 315 TGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGqiEIRPMMYLALS--YDHRLIDGKEAVTFLVTIKEL 392


                  ..
gi 954047865  361 LE 362
Cdd:TIGR01347 393 LE 394
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-362 3.79e-46

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: 165.43  E-value: 3.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865    5 KLPDLGeGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGE----- 79
Cdd:TIGR01348 120 TVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGstpat 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   80 DDGTAVGKVHGSSQVLEDHFVVGAVAA---------------GGSLTQAMPAVRRLALQLGVDVEHLKGSGPAGLVTEAD 144
Cdd:TIGR01348 199 APAPASAQPAAQSPAATQPEPAAAPAAakaqapapqqagtqnPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILRED 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  145 VQQA-----------------------------FEAQGGSHNEILKGARRAMAKAMTLSHQSVVPVTITDEVD---LRAW 192
Cdd:TIGR01348 279 VQRFvkepsvraqaaaasaaggapgalpwpnvdFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADiteMEAF 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  193 RSDED-----------VTVRLIRGIGVACRAEPSMNAWFD--GETLTRRLFdeVNVAIAVDSRHGLYVPVMENVvDRAGA 259
Cdd:TIGR01348 359 RKQQNaavekegvkltVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKY--VNIGVAVDTPNGLLVPVIKDV-DRKGI 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  260 dLRGGLDRMIADVKARA---VPREMlQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGEARPVRALPL 336
Cdd:TIGR01348 436 -TELALELSDLAKKARDgklTPDEM-QGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPL 513

                         410       420
                  ....*....|....*....|....*.
gi 954047865  337 SVTFDHRACTGGEAARFLRALVNALE 362
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLA 539
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 5-365 1.26e-43

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 159.78  E-value: 1.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   5 KLPDLGEGlaEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFE-------- 76
Cdd:PRK11854 210 NVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEvegaapaa 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  77 ------GGEDDGTAVGKVHGSSQVLEDHFVVGAVAAGGSLTQAMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQAFE 150
Cdd:PRK11854 288 apakqeAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVK 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 151 -------------AQGGSHNEILKGA------------------RRAMAKAMTLSHQSVVPVTITDEVD---LRAWR--- 193
Cdd:PRK11854 368 davkraeaapaaaAAGGGGPGLLPWPkvdfskfgeieevelgriQKISGANLHRNWVMIPHVTQFDKADiteLEAFRkqq 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 194 ------SDEDVT----VRLIRGIGVACRAEPSMNAWF--DGETLTRRlfDEVNVAIAVDSRHGLYVPVMENVVDRAGADL 261
Cdd:PRK11854 448 naeaekRKLGVKitplVFIMKAVAAALEQMPRFNSSLseDGQRLTLK--KYVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 262 rgglDRMIADV--KARA---VPREMlQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGEARPVRALPL 336
Cdd:PRK11854 526 ----SRELMDIskKARDgklTAGDM-QGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPL 600

                        410       420
                 ....*....|....*....|....*....
gi 954047865 337 SVTFDHRACTGGEAARFLRALVNALESAN 365
Cdd:PRK11854 601 SLSYDHRVIDGADGARFITIINDRLSDIR 629
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
5-362 8.62e-39

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 142.67  E-value: 8.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   5 KLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF-EGGEDDGT 83
Cdd:PRK05704   6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIdEGAAAGAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  84 AVGKVHGSSQVLEDHFVVGAVAAGGSLTQAMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQAFEAQGGSHNEilKGA 163
Cdd:PRK05704  86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA--PAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 164 RRAMAKAMTLSHQSVVPVTIT-----------------------DEVD------LRAWRSD---EDVTVRL------IRG 205
Cdd:PRK05704 164 AAPAAAPAPLGARPEERVPMTrlrktiaerlleaqnttamlttfNEVDmtpvmdLRKQYKDafeKKHGVKLgfmsffVKA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 206 IGVACRAEPSMNAWFDG-ETLTRRLFDevnVAIAVDSRHGLYVPVMENvVDRAG-ADLRGGldrmIAD--VKAR----AV 277
Cdd:PRK05704 244 VVEALKRYPEVNASIDGdDIVYHNYYD---IGIAVGTPRGLVVPVLRD-ADQLSfAEIEKK----IAElaKKARdgklSI 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 278 prEMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNG--EARPVRALPLSvtFDHRACTGGEAARFLR 355
Cdd:PRK05704 316 --EELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGqiVIRPMMYLALS--YDHRIIDGKEAVGFLV 391


                 ....*..
gi 954047865 356 ALVNALE 362
Cdd:PRK05704 392 TIKELLE 398
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 5-362 1.05e-36

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 137.12  E-value: 1.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   5 KLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGE---DD 81
Cdd:PTZ00144  48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGappAA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  82 GTAVGKVHGSSQVLEDHFVVGAVAAGGSLTQAMPAVRrlalqlgvdvehlKGSGPAGLVTEADVQQAFEAQGGSHNEI-L 160
Cdd:PTZ00144 128 APAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPA-------------AAKPPEPAPAAKPPPTPVARADPRETRVpM 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 161 KGARRAMAKAMTLSHQSVVPVTITDEVD------LRAWRSDE---DVTVRL------IRGIGVACRAEPSMNAWFDGETL 225
Cdd:PTZ00144 195 SRMRQRIAERLKASQNTCAMLTTFNECDmsalmeLRKEYKDDfqkKHGVKLgfmsafVKASTIALKKMPIVNAYIDGDEI 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 226 TRRLFdeVNVAIAVDSRHGLYVPVMENVVDRAGADLrgglDRMIAD--VKAR--AVPREMLQGATITLTNFGAIAGRYAS 301
Cdd:PTZ00144 275 VYRNY--VDISVAVATPTGLVVPVIRNCENKSFAEI----EKELADlaEKARnnKLTLEDMTGGTFTISNGGVFGSLMGT 348

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 954047865 302 PIVTPPQVTIVGAGKLFEKVVFVNGE--ARPVRALPLsvTFDHRACTGGEAARFLRALVNALE 362
Cdd:PTZ00144 349 PIINPPQSAILGMHAIKKRPVVVGNEivIRPIMYLAL--TYDHRLIDGRDAVTFLKKIKDLIE 409
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 113-363 1.09e-31

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 121.44  E-value: 1.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 113 AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQQ------------------------------AFEAQGGSHNEILKG 162
Cdd:PRK11857   4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfikslksaptpaeaasvssaqqaaktaapaAAPPKLEGKREKVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 163 ARRAMAKAMTLSHQSVVPVTITDEVDL-RAWRS----------DEDVTVR----LIRGIGVACRAEPSMNAWFDGETLTR 227
Cdd:PRK11857  84 IRKAIARAMTNSWSNVAYVNLVNEIDMtKLWDLrksvkdpvlkTEGVKLTflpfIAKAILIALKEFPIFAAKYDEATSEL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 228 RLFDEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVPREMLQGATITLTNFGAIAGRYASPIVTPP 307
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 954047865 308 QVTIVGAGKLFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALVNALES 363
Cdd:PRK11857 244 ELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEK 299
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 6-362 1.22e-28

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 116.01  E-value: 1.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   6 LPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEGGEDdgtAV 85
Cdd:PLN02226  96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED---AA 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  86 GKVHGSSQVLEDhfvVGAVAAGGSLTQAMPAVRRLALqlgvdVEHLKGSGPAGLVTEADVQQAFEAQGGSHNEILKGARR 165
Cdd:PLN02226 173 SQVTPSQKIPET---TDPKPSPPAEDKQKPKVESAPV-----AEKPKAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRK 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 166 AMAKAMTLSHQSVVPVTITDEVD------LRAWRSD---EDVTVRL------IRGIGVACRAEPSMNAWFDGETLTRRlf 230
Cdd:PLN02226 245 RVATRLKDSQNTFALLTTFNEVDmtnlmkLRSQYKDafyEKHGVKLglmsgfIKAAVSALQHQPVVNAVIDGDDIIYR-- 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 231 DEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLDRMIADVKARAVPREMLQGATITLTNFGAIAGRYASPIVTPPQVT 310
Cdd:PLN02226 323 DYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSA 402

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 954047865 311 IVGAGKLFEKVVFVNGEARPVRALPLSVTFDHRACTGGEAARFLRALVNALE 362
Cdd:PLN02226 403 ILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVE 454
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 4-75 1.27e-25

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: 98.22  E-value: 1.27e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 954047865   4 FKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:COG0508    5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 4-75 3.28e-24

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.39  E-value: 3.28e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 954047865   4 FKLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:cd06849    3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 6-362 2.46e-20

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 92.22  E-value: 2.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   6 LPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPS------------------PVSGVIANLCANEGDILH 67
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECmeegylakivkgdgakeiKVGEVIAITVEEEEDIGK 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  68 IGaplvEFEGGEDDGTAVGKVHGSSQVLEDHFV-------------VGAVAAGGSLTQAMPAVRRLALQLGVDVEHLKGS 134
Cdd:PLN02744 197 FK----DYKPSSSAAPAAPKAKPSPPPPKEEEVekpasspepkaskPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGT 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 135 GPAGLVTEADVQqAFEAQGGS---------------------HNEIlkgaRRAMAKAMTLSHQSVvP---VTITDEVD-L 189
Cdd:PLN02744 273 GPDGRIVKADIE-DYLASGGKgatappstdskapaldytdipNTQI----RKVTASRLLQSKQTI-PhyyLTVDTRVDkL 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 190 RAWRSDED------------VTVRLIRGIGVACRAEPSMNA-WFDGETltrRLFDEVNVAIAVDSRHGLYVPVMENvvdr 256
Cdd:PLN02744 347 MALRSQLNslqeasggkkisVNDLVIKAAALALRKVPQCNSsWTDDYI---RQYHNVNINVAVQTENGLYVPVVKD---- 419

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 257 agADlRGGLDRMIADVKARA-------VPREMLQGATITLTNFGAIAG-RYASPIVTPPQVTIVGAGKLFEKVVFVNGEA 328
Cdd:PLN02744 420 --AD-KKGLSTIAEEVKQLAqkarensLKPEDYEGGTFTVSNLGGPFGiKQFCAIINPPQSAILAVGSAEKRVIPGSGPD 496

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 954047865 329 RPVRALPLSVTF--DHRACTGGEAARFLRALVNALE 362
Cdd:PLN02744 497 QYNFASFMSVTLscDHRVIDGAIGAEWLKAFKGYIE 532
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 112-363 5.30e-17

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 81.10  E-value: 5.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 112 QAMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQ-----------------------QAFEAQGGSHN------EILK- 161
Cdd:PRK14843   7 RATPAARKLADDLGINLYDVSGSGANGRVHKEDVEtykdtnvvrisplakrialehniAWQEIQGTGHRgkimkkDVLAl 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 162 --------------------------------------GARRAMAKAMTLSHQSVVPVTITDEVDLR---AWR------- 193
Cdd:PRK14843  87 lpeniendsikspaqiekveevpdnvtpygeieripmtPMRKVIAQRMVESYLTAPTFTLNYEVDMTemlALRkkvlepi 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 194 ---SDEDVTVRLIRGIGV--ACRAEPSMNAWF--DGETLTrrLFDEVNVAIAVDSRHGLYVPVMENVVDRAGADLRGGLD 266
Cdd:PRK14843 167 meaTGKKTTVTDLLSLAVvkTLMKHPYINASLteDGKTII--THNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFK 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865 267 RMIAD-VKARAVPREmLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVFVNGE--ARPVRALPLsvTFDHR 343
Cdd:PRK14843 245 DVIGRtLDGKLAPSE-LQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEivIRPIMSLGL--TIDHR 321

                        330       340
                 ....*....|....*....|
gi 954047865 344 ACTGGEAARFLRALVNALES 363
Cdd:PRK14843 322 VVDGMAGAKFMKDLKELIET 341
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 4-75 3.88e-16

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: 72.25  E-value: 3.88e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 954047865    4 FKLPDLGEGLAEAeIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 5-77 1.76e-14

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 74.65  E-value: 1.76e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 954047865   5 KLPDLGEGlaEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEG 77
Cdd:PRK11854   6 KVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFES 76
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 113-146 1.91e-09

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: 52.30  E-value: 1.91e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 954047865  113 AMPAVRRLALQLGVDVEHLKGSGPAGLVTEADVQ 146
Cdd:pfam02817   3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 18-75 1.93e-09

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: 53.19  E-value: 1.93e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 954047865  18 IVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:cd06850   10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 6-75 6.23e-09

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: 52.06  E-value: 6.23e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865   6 LPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEF 75
Cdd:cd06663    4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 5-72 2.09e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.34  E-value: 2.09e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 954047865   5 KLPDLGEGLAEAEIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPL 72
Cdd:PRK14875   6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 134-366 3.99e-07

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 52.20  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  134 SGPAGLVTEADVQQAFEAQGGSHNEILKGARRAMAKAMTLSHQsvVPvTITdevdlrawrSDEDVTVRLI---------- 203
Cdd:PRK12270   94 AAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLE--VP-TAT---------SVRAVPAKLLidnrivinnh 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  204 ----RGIGV------------ACRAEPSMNAWF---DGETlTRRLFDEVNVAIAVD------SRhGLYVPVM-------- 250
Cdd:PRK12270  162 lkrtRGGKVsfthligyalvqALKAFPNMNRHYaevDGKP-TLVTPAHVNLGLAIDlpkkdgSR-QLVVPAIkgaetmdf 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  251 -------ENVVDRAgadlRGGldrmiadvKARAvprEMLQGATITLTNFGAIAGRYASPIVTPPQVTIVGAGKLFEKVVF 323
Cdd:PRK12270  240 aqfwaayEDIVRRA----RDG--------KLTA---DDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEF 304

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 954047865  324 V-NGEARPVRA-----LPLSVTFDHRACTGGEAARFLRALVNALESANG 366
Cdd:PRK12270  305 QgASEERLAELgiskvMTLTSTYDHRIIQGAESGEFLRTIHQLLLGEDG 353
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 7-74 1.50e-05

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 44.47  E-value: 1.50e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 954047865   7 PDLGEGLAEA----EIVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVE 74
Cdd:PRK05641  80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIE 151
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 23-76 2.68e-05

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: 43.35  E-value: 2.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 954047865  23 VKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFE 76
Cdd:COG0511   83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 19-55 3.34e-05

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: 42.14  E-value: 3.34e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 954047865  19 VEWKvKAGERVEVDQVLLSVETAKALVDVPSPVSGVI 55
Cdd:cd06848   34 VELP-EVGTEVKKGDPFGSVESVKAASDLYSPVSGEV 69
GcvH COG0509
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ...
 19-55 3.80e-05

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: 42.80  E-value: 3.80e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 954047865  19 VEWKvKAGERVEVDQVLLSVETAKALVDVPSPVSGVI 55
Cdd:COG0509   42 VELP-EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEV 77
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 18-77 1.01e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 44.06  E-value: 1.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 954047865  18 IVEWKVKAGERVEVDQVLLSVETAKALVDVPSPVSGVIANLCANEGDILHIGAPLVEFEG 77
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
 
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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