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Conserved domains on  [gi|2462539170|ref|XP_054231518|]
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dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sucB super family cl36875
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 16-270 5.29e-171

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]


The actual alignment was detected with superfamily member TIGR01347:

Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 478.07  E-value: 5.29e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAG--------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAF 87
Cdd:TIGR01347 143 EDIIKKTEAPASAQPPAAaaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEF 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  88 LKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITEL 167
Cdd:TIGR01347 223 EKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADL 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 168 GEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGR 247
Cdd:TIGR01347 301 GKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGK 380

                         250       260
                  ....*....|....*....|...
gi 2462539170 248 EAVTFLRKIKAAVEDPRVLLLDL 270
Cdd:TIGR01347 381 EAVTFLVTIKELLEDPRRLLLDL 403
 
Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 16-270 5.29e-171

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: 478.07  E-value: 5.29e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAG--------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAF 87
Cdd:TIGR01347 143 EDIIKKTEAPASAQPPAAaaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEF 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  88 LKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITEL 167
Cdd:TIGR01347 223 EKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADL 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 168 GEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGR 247
Cdd:TIGR01347 301 GKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGK 380

                         250       260
                  ....*....|....*....|...
gi 2462539170 248 EAVTFLRKIKAAVEDPRVLLLDL 270
Cdd:TIGR01347 381 EAVTFLVTIKELLEDPRRLLLDL 403
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 16-270 1.71e-160

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 452.21  E-value: 1.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKL 95
Cdd:PTZ00144  166 AKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  96 GFMSAFVKASAFALQEQPVVNAVIDdtTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNE 175
Cdd:PTZ00144  246 GFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNK 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 176 LAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRK 255
Cdd:PTZ00144  324 LTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKK 403

                         250
                  ....*....|....*
gi 2462539170 256 IKAAVEDPRVLLLDL 270
Cdd:PTZ00144  404 IKDLIEDPARMLLDL 418
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 55-267 9.43e-96

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 280.20  E-value: 9.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  55 LKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNlKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDI 134
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 135 SVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 214
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462539170 215 GIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLL 267
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
 
Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 16-270 5.29e-171

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: 478.07  E-value: 5.29e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAG--------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAF 87
Cdd:TIGR01347 143 EDIIKKTEAPASAQPPAAaaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEF 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  88 LKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITEL 167
Cdd:TIGR01347 223 EKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADL 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 168 GEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGR 247
Cdd:TIGR01347 301 GKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGK 380

                         250       260
                  ....*....|....*....|...
gi 2462539170 248 EAVTFLRKIKAAVEDPRVLLLDL 270
Cdd:TIGR01347 381 EAVTFLVTIKELLEDPRRLLLDL 403
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 16-270 1.71e-160

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 452.21  E-value: 1.71e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKL 95
Cdd:PTZ00144  166 AKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  96 GFMSAFVKASAFALQEQPVVNAVIDdtTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNE 175
Cdd:PTZ00144  246 GFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNK 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 176 LAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRK 255
Cdd:PTZ00144  324 LTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKK 403

                         250
                  ....*....|....*
gi 2462539170 256 IKAAVEDPRVLLLDL 270
Cdd:PTZ00144  404 IKDLIEDPARMLLDL 418
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
16-270 4.04e-150

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 425.40  E-value: 4.04e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAGK----GLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKH 91
Cdd:PRK05704  151 LAAAAAAPAAPAAAAPAAApaplGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKH 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  92 NLKLGFMSAFVKASAFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKA 171
Cdd:PRK05704  231 GVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKA 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 172 RKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVT 251
Cdd:PRK05704  309 RDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVG 388

                         250
                  ....*....|....*....
gi 2462539170 252 FLRKIKAAVEDPRVLLLDL 270
Cdd:PRK05704  389 FLVTIKELLEDPERLLLDL 407
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 21-270 6.11e-114

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 335.57  E-value: 6.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  21 PTVAPPLAEPGAGKGLRSEHREK---MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGF 97
Cdd:PLN02226  213 PSSPPPPKQSAKEPQLPPKERERrvpMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  98 MSAFVKASAFALQEQPVVNAVIDDttKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELA 177
Cdd:PLN02226  293 MSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTIS 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 178 IEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIK 257
Cdd:PLN02226  371 IDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVK 450

                         250
                  ....*....|...
gi 2462539170 258 AAVEDPRVLLLDL 270
Cdd:PLN02226  451 DVVEDPQRLLLDI 463
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 55-267 9.43e-96

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 280.20  E-value: 9.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  55 LKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNlKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDI 134
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 135 SVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 214
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462539170 215 GIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLL 267
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 18-269 1.02e-85

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 261.65  E-value: 1.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  18 AVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARhkeafLKKHNLKLGF 97
Cdd:PRK11856  167 APAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKAIGVKLTV 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  98 MSAFVKASAFALQEQPVVNAVIDDTTkeVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELA 177
Cdd:PRK11856  242 TDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLK 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 178 IEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIK 257
Cdd:PRK11856  320 PEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALK 399

                         250
                  ....*....|..
gi 2462539170 258 AAVEDPRVLLLD 269
Cdd:PRK11856  400 ELLENPALLLLE 411
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 16-268 4.30e-74

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 235.49  E-value: 4.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAGKGL----------RSEHREK-MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHK 84
Cdd:PRK11855  285 MSAAAAAAAAAAAAGGGGLGLlpwpkvdfskFGEIETKpLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLK 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  85 EAFlKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTI 164
Cdd:PRK11855  365 KEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREI 443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 165 TELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLI 244
Cdd:PRK11855  444 AELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVI 523

                         250       260
                  ....*....|....*....|....
gi 2462539170 245 DGREAVTFLRKIKAAVEDPRVLLL 268
Cdd:PRK11855  524 DGATAARFTNYLKQLLADPRRMLL 547
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 17-262 1.21e-67

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: 219.50  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  17 SAVKPTVAPPLAEPGAGKgLRSEhREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLG 96
Cdd:TIGR02927 322 APAAPAAAAKPAEPDTAK-LRGT-TQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLT 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  97 FMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNEL 176
Cdd:TIGR02927 400 FLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKL 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 177 AIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAI-----GGKVEVRPMMYVALTYDHRLIDGREAVT 251
Cdd:TIGR02927 480 KPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGR 559

                         250
                  ....*....|.
gi 2462539170 252 FLRKIKAAVED 262
Cdd:TIGR02927 560 FLTTIKKRLEE 570
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 43-268 5.67e-59

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 197.92  E-value: 5.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  43 KMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMR-ARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDD 121
Cdd:PRK11854  407 ELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRkQQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSE 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 122 TTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTP 201
Cdd:PRK11854  487 DGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTP 566

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539170 202 IINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 268
Cdd:PRK11854  567 IVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 16-266 8.53e-57

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 184.23  E-value: 8.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  16 VSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKL 95
Cdd:PRK11857   53 ASVSSAQQAAKTAAPAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  96 GFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNE 175
Cdd:PRK11857  133 TFLPFIAKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERK 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 176 LAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRK 255
Cdd:PRK11857  213 IKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASR 292

                         250
                  ....*....|.
gi 2462539170 256 IKAAVEDPRVL 266
Cdd:PRK11857  293 VKELLEKPEIL 303
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 41-268 8.08e-50

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: 171.98  E-value: 8.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  41 REKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAfLKKHNLKLGFMSAFVKASAFALQEQPVVNAVID 120
Cdd:TIGR01348 320 EVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLD 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 121 DTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISN-GGVFGSLFg 199
Cdd:TIGR01348 399 LGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSlGGIGGTAF- 477

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539170 200 TPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 268
Cdd:TIGR01348 478 TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 19-268 3.31e-49

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 168.05  E-value: 3.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  19 VKPTVAP-------PLAEPGAGKGLRSEHRE-KMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKK 90
Cdd:TIGR01349 180 QSPASANqqaaattPATYPAAAPVSTGSYEDvPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMASEV 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  91 HnlKLGFMSAFVKASAFALQEQPVVNAVIDDTTkeVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEK 170
Cdd:TIGR01349 260 Y--KLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKR 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 171 ARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGK---VEVRPMMYVALTYDHRLIDGR 247
Cdd:TIGR01349 336 ARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHRVIDGA 415

                         250       260
                  ....*....|....*....|.
gi 2462539170 248 EAVTFLRKIKAAVEDPRVLLL 268
Cdd:TIGR01349 416 VGAEFLKSFKKYLENPIEMLL 436
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 44-268 1.76e-41

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 145.43  E-value: 1.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  44 MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTT 123
Cdd:PRK14843  123 MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 124 KEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFG-SLFGtPI 202
Cdd:PRK14843  203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGvQSFG-PI 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539170 203 INPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 268
Cdd:PRK14843  282 INQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 70-270 2.71e-39

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 141.40  E-value: 2.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  70 EIDMSNIQEMRARHKEAfLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVI 149
Cdd:PLN02528  215 EINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNI 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 150 RNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRP-VAIGGKVE 228
Cdd:PLN02528  294 KNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVY 373

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462539170 229 VRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL 270
Cdd:PLN02528  374 PASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHM 415
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 102-268 1.89e-33

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 127.28  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 102 VKASAFALQEQPVVNAvidDTTKEVVyRDY--IDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIE 179
Cdd:PLN02744  372 IKAAALALRKVPQCNS---SWTDDYI-RQYhnVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPE 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170 180 DMDGGTFTISN-GGVFGSLFGTPIINPPQSAILGMhGIFDRPVAIG---GKVEVRPMMYVALTYDHRLIDGREAVTFLRK 255
Cdd:PLN02744  448 DYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAV-GSAEKRVIPGsgpDQYNFASFMSVTLSCDHRVIDGAIGAEWLKA 526

                         170
                  ....*....|...
gi 2462539170 256 IKAAVEDPRVLLL 268
Cdd:PLN02744  527 FKGYIENPESMLL 539
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 100-256 3.66e-18

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 84.17  E-value: 3.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  100 AFVKAsafaLQEQPVVNAVID--DTTKEVVYRDYIDISVAVATP-----RGLVVPVIRNVEAMNFADIERTITELGEKAR 172
Cdd:PRK12270   179 ALVQA----LKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRAR 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539170  173 KNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMhGIFDRPVAIGGKVE-------VRPMMYVALTYDHRLID 245
Cdd:PRK12270   255 DGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV-GAMEYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQ 333

                          170
                   ....*....|.
gi 2462539170  246 GREAVTFLRKI 256
Cdd:PRK12270   334 GAESGEFLRTI 344
 
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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