##gff-version 3 P50213 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 P50213 UniProtKB Chain 28 366 . . . ID=PRO_0000014436;Note=Isocitrate dehydrogenase [NAD] subunit alpha%2C mitochondrial P50213 UniProtKB Binding site 115 115 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Binding site 125 125 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Binding site 146 146 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Binding site 233 233 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Binding site 257 257 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Binding site 261 261 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Site 153 153 . . . Note=Critical for catalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28098230,ECO:0000269|PubMed:28139779;Dbxref=PMID:28098230,PMID:28139779 P50213 UniProtKB Site 200 200 . . . Note=Critical for catalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Modified residue 77 77 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D6R2 P50213 UniProtKB Modified residue 101 101 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D6R2 P50213 UniProtKB Modified residue 223 223 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D6R2 P50213 UniProtKB Modified residue 343 343 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P50213 UniProtKB Modified residue 343 343 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D6R2 P50213 UniProtKB Modified residue 350 350 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D6R2 P50213 UniProtKB Alternative sequence 1 78 . . . ID=VSP_014516;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17974005;Dbxref=PMID:17974005 P50213 UniProtKB Natural variant 122 122 . . . ID=VAR_084723;Note=In RP90%3B uncertain significance. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31012789;Dbxref=dbSNP:rs756333430,PMID:31012789 P50213 UniProtKB Natural variant 155 366 . . . ID=VAR_084724;Note=In RP90. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28412069;Dbxref=PMID:28412069 P50213 UniProtKB Natural variant 175 175 . . . ID=VAR_084725;Note=In RP90%3B uncertain significance. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28412069;Dbxref=dbSNP:rs765473830,PMID:28412069 P50213 UniProtKB Natural variant 204 204 . . . ID=VAR_084726;Note=In RP90%3B uncertain significance. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30058936;Dbxref=PMID:30058936 P50213 UniProtKB Natural variant 239 239 . . . ID=VAR_084727;Note=In RP90%3B uncertain significance. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28412069;Dbxref=dbSNP:rs2074707744,PMID:28412069 P50213 UniProtKB Natural variant 304 304 . . . ID=VAR_084728;Note=In RP90%3B uncertain significance. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28412069;Dbxref=dbSNP:rs756712426,PMID:28412069 P50213 UniProtKB Natural variant 313 313 . . . ID=VAR_084729;Note=In RP90%3B uncertain significance. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28412069;Dbxref=dbSNP:rs149862950,PMID:28412069 P50213 UniProtKB Natural variant 316 316 . . . ID=VAR_084730;Note=In RP90%3B uncertain significance. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28412069;Dbxref=dbSNP:rs770798851,PMID:28412069 P50213 UniProtKB Mutagenesis 152 152 . . . Note=No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Mutagenesis 153 153 . . . Note=Complete loss of activity of the heterotetramer%2C heterodimer composed of IDH3A and IDH3B subunits and the heterodimer composed of IDH3A and IDH3G subunits with no effect on their oligomeric states. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28139779;Dbxref=PMID:28139779 P50213 UniProtKB Mutagenesis 169 169 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Mutagenesis 200 200 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Mutagenesis 202 202 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Mutagenesis 208 208 . . . Note=Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Mutagenesis 255 255 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P50213 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6KE3 P50213 UniProtKB Helix 43 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 82 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 103 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GRU P50213 UniProtKB Helix 110 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 122 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRI P50213 UniProtKB Beta strand 141 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 149 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GRG P50213 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 164 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 173 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 194 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Turn 201 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 205 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 225 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 232 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 243 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 248 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 253 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L57 P50213 UniProtKB Beta strand 275 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 284 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 294 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Turn 297 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 305 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 321 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Beta strand 338 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRF P50213 UniProtKB Beta strand 345 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P50213 UniProtKB Helix 351 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59