##gff-version 3 O95822 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 O95822 UniProtKB Chain 40 493 . . . ID=PRO_0000021088;Note=Malonyl-CoA decarboxylase%2C mitochondrial O95822 UniProtKB Region 40 190 . . . Note=Alpha-helical domain O95822 UniProtKB Region 191 493 . . . Note=Catalytic domain O95822 UniProtKB Motif 491 493 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 O95822 UniProtKB Active site 329 329 . . . Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23791943;Dbxref=PMID:23791943 O95822 UniProtKB Active site 423 423 . . . Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23791943;Dbxref=PMID:23791943 O95822 UniProtKB Binding site 299 305 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Binding site 329 329 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Binding site 423 423 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Site 211 211 . . . Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 O95822 UniProtKB Modified residue 59 59 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Modified residue 168 168 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Modified residue 168 168 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Modified residue 211 211 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Modified residue 222 222 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Modified residue 389 389 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Modified residue 472 472 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99J39 O95822 UniProtKB Disulfide bond 206 206 . . . Note=Interchain;Ontology_term=ECO:0000255;evidence=ECO:0000255 O95822 UniProtKB Alternative sequence 1 39 . . . ID=VSP_047649;Note=In isoform Cytoplasmic+peroxisomal. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10417274,ECO:0000303|PubMed:10455107,ECO:0000303|PubMed:15489334;Dbxref=PMID:10417274,PMID:10455107,PMID:15489334 O95822 UniProtKB Mutagenesis 206 206 . . . Note=Abolishes formation of disulfide-linked homotetramers. Abolishes the cooperative enzyme kinetics that are seen under oxidative conditions. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23482565;Dbxref=PMID:23482565 O95822 UniProtKB Mutagenesis 243 243 . . . Note=Does not abolish formation of disulfide-linked homotetramers. No effect on development of cooperative enzyme kinetics in response to oxidative conditions. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23482565;Dbxref=PMID:23482565 O95822 UniProtKB Mutagenesis 290 290 . . . Note=2-fold reduction in catalytic activity. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23791943;Dbxref=PMID:23791943 O95822 UniProtKB Mutagenesis 302 302 . . . Note=Decreases catalytic activity. Increases affinity for malonyl-CoA. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23482565;Dbxref=PMID:23482565 O95822 UniProtKB Mutagenesis 329 329 . . . Note=110-fold reduction in catalytic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23791943;Dbxref=PMID:23791943 O95822 UniProtKB Mutagenesis 423 423 . . . Note=7-fold reduction in catalytic activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23791943;Dbxref=PMID:23791943 O95822 UniProtKB Mutagenesis 456 456 . . . Note=3.5-fold reduction in catalytic activity. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23791943;Dbxref=PMID:23791943 O95822 UniProtKB Sequence conflict 82 82 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Sequence conflict 119 119 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Sequence conflict 127 127 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Sequence conflict 192 192 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95822 UniProtKB Helix 40 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 67 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 81 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 99 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4F0X O95822 UniProtKB Helix 119 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 138 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4F0X O95822 UniProtKB Helix 150 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 173 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 195 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 206 214 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 224 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 235 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 250 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 266 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 285 294 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Turn 299 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4F0X O95822 UniProtKB Helix 303 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 324 327 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 334 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 348 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4F0X O95822 UniProtKB Helix 357 367 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4F0X O95822 UniProtKB Helix 374 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Turn 380 382 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 383 386 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 388 393 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 395 407 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 414 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 418 425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 429 434 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 441 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Beta strand 451 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 458 460 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 461 471 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW O95822 UniProtKB Helix 478 486 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YGW