##gff-version 3 P07954 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10173 P07954 UniProtKB Chain 45 510 . . . ID=PRO_0000010319;Note=Fumarate hydratase%2C mitochondrial P07954 UniProtKB Active site 235 235 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05042 P07954 UniProtKB Active site 365 365 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WN93 P07954 UniProtKB Binding site 145 147 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05042 P07954 UniProtKB Binding site 176 179 . . . Note=In site B;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05042 P07954 UniProtKB Binding site 186 188 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05042 P07954 UniProtKB Binding site 234 234 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WN93 P07954 UniProtKB Binding site 366 366 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WN93 P07954 UniProtKB Binding site 371 373 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WN93 P07954 UniProtKB Site 378 378 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05042 P07954 UniProtKB Modified residue 61 61 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 61 61 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 66 66 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P07954 UniProtKB Modified residue 66 66 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 80 80 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P07954 UniProtKB Modified residue 80 80 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 85 85 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 90 90 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P07954 UniProtKB Modified residue 94 94 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P07954 UniProtKB Modified residue 115 115 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 115 115 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 122 122 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 122 122 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 213 213 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 223 223 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 223 223 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 236 236 . . . Note=Phosphothreonine%3B by PRKDC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26237645;Dbxref=PMID:26237645 P07954 UniProtKB Modified residue 256 256 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P07954 UniProtKB Modified residue 292 292 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P07954 UniProtKB Modified residue 292 292 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 366 366 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P07954 UniProtKB Modified residue 467 467 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 473 473 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Modified residue 502 502 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97807 P07954 UniProtKB Alternative sequence 1 43 . . . ID=VSP_018965;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27037871;Dbxref=PMID:27037871 P07954 UniProtKB Natural variant 107 107 . . . ID=VAR_013497;Note=In HLRCC. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11865300;Dbxref=dbSNP:rs121913121,PMID:11865300 P07954 UniProtKB Natural variant 117 117 . . . ID=VAR_013498;Note=In HLRCC. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11865300;Dbxref=dbSNP:rs886039363,PMID:11865300 P07954 UniProtKB Natural variant 180 180 . . . ID=VAR_013499;Note=In HLRCC. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11865300;Dbxref=dbSNP:rs863224015,PMID:11865300 P07954 UniProtKB Natural variant 185 185 . . . ID=VAR_013500;Note=In HLRCC. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11865300;Dbxref=dbSNP:rs779707997,PMID:11865300 P07954 UniProtKB Natural variant 230 230 . . . ID=VAR_002445;Note=In FMRD and HLRCC. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11865300,ECO:0000269|PubMed:9635293;Dbxref=dbSNP:rs752232718,PMID:11865300,PMID:9635293 P07954 UniProtKB Natural variant 233 233 . . . ID=VAR_013501;Note=In HLRCC%3B catalytically inactive mutant%3B abolished ability to promote DNA repair. R->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11865300,ECO:0000269|PubMed:26237645;Dbxref=dbSNP:rs121913123,PMID:11865300,PMID:26237645 P07954 UniProtKB Natural variant 282 282 . . . ID=VAR_013502;Note=In HLRCC. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11865300;Dbxref=dbSNP:rs935002190,PMID:11865300 P07954 UniProtKB Natural variant 308 308 . . . ID=VAR_002446;Note=In FMRD. A->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9635293,ECO:0000269|Ref.23;Dbxref=dbSNP:rs121913118,PMID:9635293 P07954 UniProtKB Natural variant 312 312 . . . ID=VAR_002447;Note=In FMRD. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9635293;Dbxref=dbSNP:rs1553341046,PMID:9635293 P07954 UniProtKB Natural variant 328 328 . . . ID=VAR_013503;Note=In HLRCC. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11865300;Dbxref=PMID:11865300 P07954 UniProtKB Natural variant 362 362 . . . ID=VAR_081606;Note=In HLRCC. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8200987;Dbxref=dbSNP:rs121913119,PMID:8200987 P07954 UniProtKB Natural variant 425 425 . . . ID=VAR_002448;Note=In FMRD. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9635293;Dbxref=PMID:9635293 P07954 UniProtKB Mutagenesis 46 46 . . . Note=Does not affect phosphorylation by PRKDC. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26237645;Dbxref=PMID:26237645 P07954 UniProtKB Mutagenesis 147 147 . . . Note=Does not affect phosphorylation by PRKDC. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26237645;Dbxref=PMID:26237645 P07954 UniProtKB Mutagenesis 187 187 . . . Note=Does not affect phosphorylation by PRKDC. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26237645;Dbxref=PMID:26237645 P07954 UniProtKB Mutagenesis 236 236 . . . Note=Abolished interaction with H2AZ1 and localization to chromatin in response to DNA damage. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26237645;Dbxref=PMID:26237645 P07954 UniProtKB Mutagenesis 236 236 . . . Note=Phosphomimetic mutant%3B promotes interaction with H2AZ1%2C leading to increased localization to chromatin in response to DNA damage. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26237645;Dbxref=PMID:26237645 P07954 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 58 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 70 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 90 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 108 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 114 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Turn 129 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VBE P07954 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 139 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 147 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 177 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Turn 182 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 190 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 207 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Turn 225 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 229 234 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 237 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 244 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Turn 267 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Turn 277 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 289 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 311 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 319 345 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 349 352 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 366 368 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3E04 P07954 UniProtKB Helix 375 399 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 409 433 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 435 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 442 451 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 454 459 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 460 463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 465 478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 482 488 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 494 500 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Helix 503 505 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Beta strand 506 508 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UPP P07954 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27037871;Dbxref=PMID:27037871