##gff-version 3 Q9BV79 UniProtKB Transit peptide 1 53 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BV79 UniProtKB Chain 54 373 . . . ID=PRO_0000000888;Note=Enoyl-[acyl-carrier-protein] reductase%2C mitochondrial Q9BV79 UniProtKB Active site 94 94 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Binding site 167 167 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Binding site 193 196 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Binding site 216 218 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Binding site 285 288 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Binding site 310 312 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Binding site 368 368 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 Q9BV79 UniProtKB Modified residue 61 61 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Modified residue 61 61 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Modified residue 252 252 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Modified residue 252 252 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Modified residue 267 267 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Modified residue 267 267 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Modified residue 316 316 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DCS3 Q9BV79 UniProtKB Alternative sequence 1 76 . . . ID=VSP_041131;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9BV79 UniProtKB Natural variant 96 96 . . . ID=VAR_027935;Note=F->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10810093,ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|Ref.3,ECO:0000269|Ref.5;Dbxref=dbSNP:rs1128400,PMID:10810093,PMID:14702039,PMID:15489334 Q9BV79 UniProtKB Natural variant 227 227 . . . ID=VAR_055486;Note=R->K;Dbxref=dbSNP:rs11544658 Q9BV79 UniProtKB Natural variant 232 232 . . . ID=VAR_077997;Note=In DYTOABG%3B probably decreased protein abundance. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27817865;Dbxref=dbSNP:rs762913101,PMID:27817865 Q9BV79 UniProtKB Natural variant 258 258 . . . ID=VAR_055487;Note=R->L;Dbxref=dbSNP:rs34835902 Q9BV79 UniProtKB Natural variant 258 258 . . . ID=VAR_077998;Note=In DYTOABG. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27817865;Dbxref=dbSNP:rs145192716,PMID:27817865 Q9BV79 UniProtKB Natural variant 285 373 . . . ID=VAR_077999;Note=In DYTOABG%3B probably decreased protein abundance. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27817865;Dbxref=PMID:27817865 Q9BV79 UniProtKB Natural variant 285 285 . . . ID=VAR_078000;Note=In DYTOABG. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27817865;Dbxref=dbSNP:rs759218713,PMID:27817865 Q9BV79 UniProtKB Mutagenesis 85 85 . . . Note=Reduces catalytic activity by 68%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 94 94 . . . Note=Reduces catalytic activity by 95%25. Strongly reduces affinity for trans-oct-2-enoyl-CoA. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 129 129 . . . Note=Strongly increases activity with trans-oct-2-enoyl-CoA. No effect on activity with trans-tetradec-2-enoyl-CoA. Decreases activity with trans-hexadec-2-enoyl-CoA by 20%25. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 165 165 . . . Note=Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 73%25. Decreases activity with trans-hexadec-2-enoyl-CoA by 80%25. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 170 170 . . . Note=Reduces catalytic activity by 69%25. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 311 311 . . . Note=Reduces catalytic activity by 98%25. Strongly reduces affinity for trans-oct-2-enoyl-CoA. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 311 311 . . . Note=Reduces catalytic activity by 87%25. Strongly reduces affinity for trans-oct-2-enoyl-CoA. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Mutagenesis 324 324 . . . Note=Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 25%25. Decreases activity with trans-hexadec-2-enoyl-CoA by 68%25. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18479707;Dbxref=PMID:18479707 Q9BV79 UniProtKB Sequence conflict 45 46 . . . Note=AL->GV;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BV79 UniProtKB Sequence conflict 373 373 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BV79 UniProtKB Beta strand 43 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 54 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 58 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 72 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 84 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 127 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 138 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 149 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 154 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 158 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 167 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 186 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 195 207 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 210 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 221 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 234 238 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 239 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 245 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 252 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 266 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 281 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VCY Q9BV79 UniProtKB Helix 297 302 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 306 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 312 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 321 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 345 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 350 352 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Helix 353 360 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY Q9BV79 UniProtKB Beta strand 366 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ZSY