##gff-version 3 P16219 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1286669;Dbxref=PMID:1286669 P16219 UniProtKB Chain 25 412 . . . ID=PRO_0000000498;Note=Short-chain specific acyl-CoA dehydrogenase%2C mitochondrial P16219 UniProtKB Active site 392 392 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15651 P16219 UniProtKB Binding site 152 161 . . . Note=In other chain;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10 P16219 UniProtKB Binding site 161 161 . . . . P16219 UniProtKB Binding site 185 187 . . . Note=In other chain;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10 P16219 UniProtKB Binding site 269 272 . . . . P16219 UniProtKB Binding site 297 297 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10 P16219 UniProtKB Binding site 308 308 . . . Note=In other chain;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10 P16219 UniProtKB Binding site 365 369 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10 P16219 UniProtKB Binding site 393 393 . . . . P16219 UniProtKB Binding site 394 396 . . . Note=In other chain;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10 P16219 UniProtKB Modified residue 27 27 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 51 51 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 51 51 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 72 72 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 129 129 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 129 129 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 208 208 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 262 262 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 262 262 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 306 306 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Modified residue 306 306 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q07417 P16219 UniProtKB Natural variant 46 46 . . . ID=VAR_000310;Note=In ACADSD. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1692038;Dbxref=dbSNP:rs121908003,PMID:1692038 P16219 UniProtKB Natural variant 90 90 . . . ID=VAR_013565;Note=In ACADSD%3B loss of acyl-CoA dehydrogenase activity. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11134486;Dbxref=dbSNP:rs121908005,PMID:11134486 P16219 UniProtKB Natural variant 92 92 . . . ID=VAR_000311;Note=In ACADSD. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9499414;Dbxref=dbSNP:rs121908004,PMID:9499414 P16219 UniProtKB Natural variant 104 104 . . . ID=VAR_013566;Note=In ACADSD%3B loss of acyl-CoA dehydrogenase activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11134486;Dbxref=dbSNP:rs387906308,PMID:11134486 P16219 UniProtKB Natural variant 107 107 . . . ID=VAR_000312;Note=In ACADSD. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1692038;Dbxref=dbSNP:rs61732144,PMID:1692038 P16219 UniProtKB Natural variant 171 171 . . . ID=VAR_013567;Note=69%25 of wild-type acyl-CoA dehydrogenase activity%3B confers susceptibility to ethylmalonicaciduria. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11134486,ECO:0000269|PubMed:9499414;Dbxref=dbSNP:rs1800556,PMID:11134486,PMID:9499414 P16219 UniProtKB Natural variant 177 177 . . . ID=VAR_000314;Note=In ACADSD. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9499414;Dbxref=dbSNP:rs57443665,PMID:9499414 P16219 UniProtKB Natural variant 192 192 . . . ID=VAR_013568;Note=In ACADSD%3B loss of acyl-CoA dehydrogenase activity. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11134486;Dbxref=dbSNP:rs28940874,PMID:11134486 P16219 UniProtKB Natural variant 209 209 . . . ID=VAR_000315;Note=86%25 of wild-type acyl-CoA dehydrogenase activity%3B confers susceptibility to ethylmalonicaciduria. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11134486,ECO:0000269|PubMed:9499414;Dbxref=dbSNP:rs1799958,PMID:11134486,PMID:9499414 P16219 UniProtKB Natural variant 325 325 . . . ID=VAR_013569;Note=In ACADSD%3B loss of acyl-CoA dehydrogenase activity. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11134486;Dbxref=dbSNP:rs121908006,PMID:11134486 P16219 UniProtKB Natural variant 353 353 . . . ID=VAR_013570;Note=In ACADSD%3B loss of acyl-CoA dehydrogenase activity. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11134486;Dbxref=dbSNP:rs28941773,PMID:11134486 P16219 UniProtKB Natural variant 380 380 . . . ID=VAR_013571;Note=In ACADSD%3B loss of acyl-CoA dehydrogenase activity. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11134486;Dbxref=dbSNP:rs28940875,PMID:11134486 P16219 UniProtKB Natural variant 383 383 . . . ID=VAR_000316;Note=In ACADSD. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9499414;Dbxref=dbSNP:rs28940872,PMID:9499414 P16219 UniProtKB Natural variant 383 383 . . . ID=VAR_033458;Note=R->H;Dbxref=dbSNP:rs35233375 P16219 UniProtKB Helix 36 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Turn 53 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 57 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 68 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 86 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 95 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 110 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 133 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 141 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 144 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 150 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 159 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 176 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Turn 188 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 193 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 203 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 210 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 238 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 250 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Beta strand 253 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 260 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 304 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 308 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 342 367 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 368 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 378 388 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Turn 389 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG P16219 UniProtKB Helix 395 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VIG