##gff-version 3 P40926 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00346 P40926 UniProtKB Chain 25 338 . . . ID=PRO_0000018628;Note=Malate dehydrogenase%2C mitochondrial P40926 UniProtKB Active site 200 200 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00346 P40926 UniProtKB Binding site 31 37 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.16 P40926 UniProtKB Binding site 57 57 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.16 P40926 UniProtKB Binding site 104 104 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10004,ECO:0000269|Ref.16 P40926 UniProtKB Binding site 110 110 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10004,ECO:0000269|Ref.16 P40926 UniProtKB Binding site 117 117 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.16 P40926 UniProtKB Binding site 140 142 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.16 P40926 UniProtKB Binding site 142 142 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10004,ECO:0000269|Ref.16 P40926 UniProtKB Binding site 176 176 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10004,ECO:0000269|Ref.16 P40926 UniProtKB Binding site 251 251 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.16 P40926 UniProtKB Modified residue 78 78 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 78 78 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 91 91 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 91 91 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 165 165 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P40926 UniProtKB Modified residue 185 185 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20167786,ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861,PMID:20167786 P40926 UniProtKB Modified residue 185 185 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 203 203 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 215 215 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 215 215 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 239 239 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 239 239 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q32LG3 P40926 UniProtKB Modified residue 239 239 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q32LG3 P40926 UniProtKB Modified residue 246 246 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P40926 UniProtKB Modified residue 269 269 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 296 296 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 296 296 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 301 301 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20167786,ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861,PMID:20167786 P40926 UniProtKB Modified residue 301 301 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q32LG3 P40926 UniProtKB Modified residue 307 307 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 P40926 UniProtKB Modified residue 307 307 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21908771;Dbxref=PMID:21908771 P40926 UniProtKB Modified residue 307 307 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 314 314 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20167786,ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861,PMID:20167786 P40926 UniProtKB Modified residue 314 314 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 324 324 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 324 324 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P40926 UniProtKB Modified residue 328 328 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q32LG3 P40926 UniProtKB Modified residue 328 328 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q32LG3 P40926 UniProtKB Modified residue 329 329 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P40926 UniProtKB Modified residue 329 329 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q32LG3 P40926 UniProtKB Modified residue 335 335 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P40926 UniProtKB Modified residue 335 335 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08249 P40926 UniProtKB Glycosylation 33 33 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04636 P40926 UniProtKB Alternative sequence 144 185 . . . ID=VSP_055312;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P40926 UniProtKB Natural variant 9 9 . . . ID=VAR_047787;Note=A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|Ref.1;Dbxref=dbSNP:rs6720,PMID:15489334 P40926 UniProtKB Natural variant 37 37 . . . ID=VAR_078001;Note=In DEE51%3B severe defects in aerobic respiration%2C when assayed in a heterologous system. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27989324;Dbxref=dbSNP:rs782308462,PMID:27989324 P40926 UniProtKB Natural variant 133 133 . . . ID=VAR_078002;Note=In DEE51%3B decreased protein abundance%3B strong decrease in malate dehydrogenase activity%3B severe defects in aerobic respiration%2C when assayed in a heterologous system. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27989324;Dbxref=dbSNP:rs375002796,PMID:27989324 P40926 UniProtKB Natural variant 207 207 . . . ID=VAR_078003;Note=In DEE51%3B decreased protein abundance%3B strong decrease in malate dehydrogenase activity%3B severe defects in aerobic respiration%2C when assayed in a heterologous system. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27989324;Dbxref=dbSNP:rs1057519566,PMID:27989324 P40926 UniProtKB Mutagenesis 185 185 . . . Note=No activation of enzyme activity on treatment with TSA or NAM%3B when associated with R-301%3B R-307 and R-314. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 P40926 UniProtKB Mutagenesis 301 301 . . . Note=No activation of enzyme activity on treatment with TSA or NAM%3B when associated with R-185%3B R-307 and R-314. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 P40926 UniProtKB Mutagenesis 307 307 . . . Note=No activation of enzyme activity on treatment with TSA or NAM%3B when associated with R-185%3B R-301 and R-314. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 P40926 UniProtKB Mutagenesis 314 314 . . . Note=No activation of enzyme activity on treatment with TSA or NAM%3B when associated with R-185%3B R-301 and R-307. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 P40926 UniProtKB Sequence conflict 301 301 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P40926 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Turn 31 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 37 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 50 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 61 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 71 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 76 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 86 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 94 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 110 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 114 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 135 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 144 157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 171 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 189 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 220 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 249 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 282 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Beta strand 298 302 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD P40926 UniProtKB Helix 310 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DFD