##gff-version 3 P09622 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 P09622 UniProtKB Chain 36 509 . . . ID=PRO_0000030295;Note=Dihydrolipoyl dehydrogenase%2C mitochondrial P09622 UniProtKB Active site 487 487 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09624 P09622 UniProtKB Binding site 71 80 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 89 89 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 154 154 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 183 185 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 220 227 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 243 243 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 278 278 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 314 314 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 355 355 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Binding site 361 364 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15946682;Dbxref=PMID:15946682 P09622 UniProtKB Site 448 448 . . . Note=Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Site 473 473 . . . Note=Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Modified residue 66 66 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 66 66 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 104 104 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 104 104 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 122 122 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 122 122 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 132 132 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 132 132 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 143 143 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09622 UniProtKB Modified residue 143 143 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 159 159 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 166 166 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 273 273 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 277 277 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6P6R2 P09622 UniProtKB Modified residue 346 346 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 410 410 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09622 UniProtKB Modified residue 410 410 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 417 417 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09622 UniProtKB Modified residue 420 420 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 430 430 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P09622 UniProtKB Modified residue 505 505 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Modified residue 505 505 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08749 P09622 UniProtKB Disulfide bond 80 85 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09624 P09622 UniProtKB Alternative sequence 1 99 . . . ID=VSP_055855;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P09622 UniProtKB Alternative sequence 147 194 . . . ID=VSP_055856;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P09622 UniProtKB Natural variant 47 47 . . . ID=VAR_076985;Note=In DLDD. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16770810;Dbxref=dbSNP:rs397514651,PMID:16770810 P09622 UniProtKB Natural variant 72 72 . . . ID=VAR_006907;Note=In DLDD%3B reduced dihydrolipoyl dehydrogenase activity%3B no effect on interaction with PDHX. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20160912,ECO:0000269|PubMed:8506365;Dbxref=dbSNP:rs121964987,PMID:20160912,PMID:8506365 P09622 UniProtKB Natural variant 104 104 . . . ID=VAR_031922;Note=K->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3693355,ECO:0000269|PubMed:8406489;Dbxref=dbSNP:rs1130477,PMID:3693355,PMID:8406489 P09622 UniProtKB Natural variant 136 136 . . . ID=VAR_076986;Note=In DLDD. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9540846;Dbxref=PMID:9540846 P09622 UniProtKB Natural variant 229 229 . . . ID=VAR_015820;Note=In DLDD. G->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16770810,ECO:0000269|PubMed:9934985;Dbxref=dbSNP:rs121964990,PMID:16770810,PMID:9934985 P09622 UniProtKB Natural variant 331 331 . . . ID=VAR_014555;Note=L->V;Dbxref=dbSNP:rs17624 P09622 UniProtKB Natural variant 361 361 . . . ID=VAR_076987;Note=In DLDD. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11687750;Dbxref=dbSNP:rs121964993,PMID:11687750 P09622 UniProtKB Natural variant 375 375 . . . ID=VAR_076988;Note=In DLDD%3B loss of enzyme activity%3B abolished interaction with PDHX. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11687750,ECO:0000269|PubMed:16770810,ECO:0000269|PubMed:20160912,ECO:0000269|PubMed:9540846;Dbxref=dbSNP:rs121964992,PMID:11687750,PMID:16770810,PMID:20160912,PMID:9540846 P09622 UniProtKB Natural variant 393 393 . . . ID=VAR_076989;Note=In DLDD. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12925875;Dbxref=dbSNP:rs121964991,PMID:12925875 P09622 UniProtKB Natural variant 479 479 . . . ID=VAR_076990;Note=In DLDD%3B reduced dehydrogenase activity%3B increased proteolytic activity. D->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10448086,ECO:0000269|PubMed:17404228;Dbxref=dbSNP:rs397514649,PMID:10448086,PMID:17404228 P09622 UniProtKB Natural variant 482 482 . . . ID=VAR_076991;Note=In DLDD%3B reduced enzyme activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15712224;Dbxref=dbSNP:rs397514650,PMID:15712224 P09622 UniProtKB Natural variant 488 488 . . . ID=VAR_006908;Note=In DLDD%3B no effect on interaction with PDHX. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20160912,ECO:0000269|PubMed:8506365;Dbxref=dbSNP:rs121964988,PMID:20160912,PMID:8506365 P09622 UniProtKB Natural variant 495 495 . . . ID=VAR_015821;Note=In DLDD%3B loss of enzyme activity%3B reduced interaction with PDHX. R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16442803,ECO:0000269|PubMed:20160912,ECO:0000269|PubMed:8968745;Dbxref=dbSNP:rs121964989,PMID:16442803,PMID:20160912,PMID:8968745 P09622 UniProtKB Mutagenesis 89 89 . . . Note=Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20160912;Dbxref=PMID:20160912 P09622 UniProtKB Mutagenesis 383 383 . . . Note=Reduces dihydrolipoyl dehydrogenase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 383 383 . . . Note=Reduces dihydrolipoyl dehydrogenase activity. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 448 448 . . . Note=Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 448 448 . . . Note=Does not affect dihydrolipoyl dehydrogenase activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 466 466 . . . Note=Decreases dehydrogenase activity. Loss of proteolytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17404228;Dbxref=PMID:17404228 P09622 UniProtKB Mutagenesis 473 473 . . . Note=Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 473 473 . . . Note=Does not affect dihydrolipoyl dehydrogenase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 473 473 . . . Note=Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 482 482 . . . Note=Does not affect dihydrolipoyl dehydrogenase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20385101;Dbxref=PMID:20385101 P09622 UniProtKB Mutagenesis 482 482 . . . Note=Does not affect interaction with PDHX. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20160912;Dbxref=PMID:20160912 P09622 UniProtKB Mutagenesis 485 485 . . . Note=Loss of dehydrogenase activity. Increases proteolytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17404228;Dbxref=PMID:17404228 P09622 UniProtKB Mutagenesis 491 491 . . . Note=Loss of proteolytic activity. Does not affect dehydrogenase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17404228;Dbxref=PMID:17404228 P09622 UniProtKB Mutagenesis 492 492 . . . Note=Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20160912;Dbxref=PMID:20160912 P09622 UniProtKB Mutagenesis 505 505 . . . Note=Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20160912;Dbxref=PMID:20160912 P09622 UniProtKB Sequence conflict 154 154 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09622 UniProtKB Sequence conflict 209 209 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09622 UniProtKB Sequence conflict 493 493 . . . Note=A->AEA;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09622 UniProtKB Beta strand 40 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 51 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 67 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 78 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 85 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 105 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 120 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 148 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 171 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 197 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 203 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 214 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 223 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 238 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 244 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 255 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 271 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 275 283 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 289 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 302 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 315 317 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 324 327 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 350 352 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 354 356 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 357 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 363 377 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 386 388 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 391 393 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 395 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 406 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 416 422 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 423 425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 427 432 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 438 444 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Turn 445 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Beta strand 449 457 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 460 473 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 477 482 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R P09622 UniProtKB Helix 491 503 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I4R