##gff-version 3 Q39219 UniProtKB Transit peptide 1 62 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q39219 UniProtKB Chain 63 354 . . . ID=PRO_0000001731;Note=Ubiquinol oxidase 1a%2C mitochondrial Q39219 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q39219 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q39219 UniProtKB Region 68 99 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q39219 UniProtKB Compositional bias 71 85 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q39219 UniProtKB Binding site 183 183 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 222 222 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 222 222 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 225 225 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 273 273 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 324 324 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 324 324 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Binding site 327 327 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26710 Q39219 UniProtKB Disulfide bond 127 127 . . . Note=Interchain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9804851;Dbxref=PMID:9804851 Q39219 UniProtKB Mutagenesis 127 127 . . . Note=Loss of activity and stimulation by pyruvate. C->A%2CL%2CQ;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10431811,ECO:0000269|PubMed:12034477,ECO:0000269|PubMed:9804851;Dbxref=PMID:10431811,PMID:12034477,PMID:9804851 Q39219 UniProtKB Mutagenesis 127 127 . . . Note=Active enzyme insensitive to stimulation by pyruvate. C->E%2CD%2CR%2CK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10431811,ECO:0000269|PubMed:12034477,ECO:0000269|PubMed:9804851;Dbxref=PMID:10431811,PMID:12034477,PMID:9804851 Q39219 UniProtKB Mutagenesis 127 127 . . . Note=Loss of oxidative inactivation and stimulation by pyruvate%2C but can be activated by succinate. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10431811,ECO:0000269|PubMed:12034477,ECO:0000269|PubMed:9804851;Dbxref=PMID:10431811,PMID:12034477,PMID:9804851 Q39219 UniProtKB Mutagenesis 177 177 . . . Note=No effect on stimulation by pyruvate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9804851;Dbxref=PMID:9804851 Q39219 UniProtKB Mutagenesis 264 264 . . . Note=Increased resistance to a substrate-analog inhibitor. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9554960;Dbxref=PMID:9554960 Q39219 UniProtKB Mutagenesis 268 268 . . . Note=Increased resistance to a substrate-analog inhibitor. M->I%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9554960;Dbxref=PMID:9554960 Q39219 UniProtKB Mutagenesis 352 352 . . . Note=Increased resistance to a substrate-analog inhibitor. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9554960;Dbxref=PMID:9554960 Q39219 UniProtKB Sequence conflict 37 37 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q39219 UniProtKB Sequence conflict 50 51 . . . Note=IW->MD;Ontology_term=ECO:0000305;evidence=ECO:0000305