##gff-version 3 P51553 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51553 UniProtKB Chain 40 393 . . . ID=PRO_0000014449;Note=Isocitrate dehydrogenase [NAD] subunit gamma%2C mitochondrial P51553 UniProtKB Binding site 120 120 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 133 133 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 136 136 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 167 167 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 312 312 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 313 313 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Binding site 324 324 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Alternative sequence 361 393 . . . ID=VSP_046771;Note=In isoform 2. MHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA->VRFPSHPTLLPRPVSPCSLL;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51553 UniProtKB Mutagenesis 117 117 . . . Note=No effect on 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 P51553 UniProtKB Mutagenesis 120 120 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 130 130 . . . Note=No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 133 133 . . . 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 P51553 UniProtKB Mutagenesis 136 136 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 167 167 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 173 173 . . . Note=No 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 P51553 UniProtKB Mutagenesis 174 174 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 190 190 . . . Note=Complete loss of the activation of the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28098230,ECO:0000269|PubMed:28139779;Dbxref=PMID:28098230,PMID:28139779 P51553 UniProtKB Mutagenesis 229 229 . . . Note=Significantly impairs 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 P51553 UniProtKB Mutagenesis 276 276 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 311 311 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 312 312 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 313 313 . . . Note=Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 315 315 . . . Note=No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Mutagenesis 324 324 . . . Note=Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28098230;Dbxref=PMID:28098230 P51553 UniProtKB Sequence conflict 267 267 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51553 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 66 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 83 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 98 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 131 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRH P51553 UniProtKB Beta strand 162 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 178 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 185 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 194 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 215 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 228 240 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 246 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 253 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 264 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 268 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 274 288 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Turn 291 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 295 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Beta strand 304 308 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 315 317 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Turn 318 321 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L57 P51553 UniProtKB Helix 326 338 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 342 356 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 364 366 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Helix 372 382 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6L59 P51553 UniProtKB Turn 384 386 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GRH P51553 UniProtKB Beta strand 389 391 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GRG