##gff-version 3 P05062 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250,ECO:0000269;evidence=ECO:0000250|UniProtKB:Q91Y97,ECO:0000269|PubMed:2649152;Dbxref=PMID:2649152 P05062 UniProtKB Chain 2 364 . . . ID=PRO_0000216940;Note=Fructose-bisphosphate aldolase B P05062 UniProtKB Active site 188 188 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P05062 UniProtKB Active site 230 230 . . . Note=Schiff-base intermediate with dihydroxyacetone-P;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P05062 UniProtKB Binding site 43 43 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P05062 UniProtKB Binding site 272 274 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P05062 UniProtKB Binding site 304 304 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P05062 UniProtKB Site 364 364 . . . Note=Necessary for preference for fructose 1%2C6-bisphosphate over fructose 1-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P05062 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P05062 UniProtKB Modified residue 13 13 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P05062 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 39 39 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 119 119 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 121 121 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P05062 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00884 P05062 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00884 P05062 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P05062 UniProtKB Modified residue 317 317 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P05062 UniProtKB Natural variant 46 46 . . . ID=VAR_075348;Note=In HFI%3B reduced enzymatic activity. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20848650;Dbxref=dbSNP:rs41281039,PMID:20848650 P05062 UniProtKB Natural variant 74 74 . . . ID=VAR_020822;Note=In HFI%3B affects proper folding. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15532022;Dbxref=dbSNP:rs781023784,PMID:15532022 P05062 UniProtKB Natural variant 120 121 . . . ID=VAR_020823;Note=In HFI. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15532022;Dbxref=PMID:15532022 P05062 UniProtKB Natural variant 134 134 . . . ID=VAR_038429;Note=R->S;Dbxref=dbSNP:rs10123355 P05062 UniProtKB Natural variant 135 135 . . . ID=VAR_000551;Note=In HFI%3B America%3B partial activity. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8299883;Dbxref=PMID:8299883 P05062 UniProtKB Natural variant 148 148 . . . ID=VAR_000552;Note=In one subject with fructose intolerance%3B rare variant%3B America. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7717389;Dbxref=dbSNP:rs118204430,PMID:7717389 P05062 UniProtKB Natural variant 150 150 . . . ID=VAR_000553;Note=In HFI%3B frequent mutation. A->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024431,ECO:0000269|PubMed:12205126,ECO:0000269|PubMed:15532022,ECO:0000269|PubMed:15880727,ECO:0000269|PubMed:20848650,ECO:0000269|PubMed:3383242;Dbxref=dbSNP:rs1800546,PMID:10024431,PMID:12205126,PMID:15532022,PMID:15880727,PMID:20848650,PMID:3383242 P05062 UniProtKB Natural variant 175 175 . . . ID=VAR_000554;Note=In HFI%3B frequent mutation. A->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024431,ECO:0000269|PubMed:12205126,ECO:0000269|PubMed:15532022,ECO:0000269|PubMed:15880727,ECO:0000269|PubMed:1967768,ECO:0000269|PubMed:20848650;Dbxref=dbSNP:rs76917243,PMID:10024431,PMID:12205126,PMID:15532022,PMID:15880727,PMID:1967768,PMID:20848650 P05062 UniProtKB Natural variant 178 178 . . . ID=VAR_058211;Note=In HFI. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15880727;Dbxref=PMID:15880727 P05062 UniProtKB Natural variant 185 185 . . . ID=VAR_020824;Note=In HFI. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12205126;Dbxref=PMID:12205126 P05062 UniProtKB Natural variant 207 207 . . . ID=VAR_020825;Note=E->Q;Dbxref=dbSNP:rs3739721 P05062 UniProtKB Natural variant 222 222 . . . ID=VAR_020826;Note=In HFI%3B affects proper folding. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15532022;Dbxref=dbSNP:rs1554702442,PMID:15532022 P05062 UniProtKB Natural variant 229 229 . . . ID=VAR_020827;Note=In HFI%3B affects proper folding. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15532022;Dbxref=dbSNP:rs1554702433,PMID:15532022 P05062 UniProtKB Natural variant 257 257 . . . ID=VAR_000555;Note=In HFI%3B Italy. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024431,ECO:0000269|PubMed:15532022,ECO:0000269|PubMed:8162030;Dbxref=dbSNP:rs764701775,PMID:10024431,PMID:15532022,PMID:8162030 P05062 UniProtKB Natural variant 268 268 . . . ID=VAR_038430;Note=I->N;Dbxref=dbSNP:rs10989495 P05062 UniProtKB Natural variant 284 284 . . . ID=VAR_058212;Note=In HFI. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15880727;Dbxref=PMID:15880727 P05062 UniProtKB Natural variant 304 304 . . . ID=VAR_020828;Note=In HFI%3B 100-fold decrease in catalytic efficiency for substrates F1%2C6BP and F1P. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10970798;Dbxref=dbSNP:rs145078268,PMID:10970798 P05062 UniProtKB Natural variant 304 304 . . . ID=VAR_000556;Note=In HFI%3B Turkey%3B 4800-fold decrease in catalytic efficiency for F1%2C6BP and inactive with F1P. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024431,ECO:0000269|PubMed:10970798;Dbxref=dbSNP:rs555935217,PMID:10024431,PMID:10970798 P05062 UniProtKB Natural variant 335 335 . . . ID=VAR_000557;Note=In HFI%3B frequent mutation. N->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024431,ECO:0000269|PubMed:12205126,ECO:0000269|PubMed:15532022,ECO:0000269|PubMed:15880727,ECO:0000269|PubMed:2336380;Dbxref=dbSNP:rs78340951,PMID:10024431,PMID:12205126,PMID:15532022,PMID:15880727,PMID:2336380 P05062 UniProtKB Natural variant 338 338 . . . ID=VAR_000558;Note=In HFI%3B Turkey and South Europe. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024431,ECO:0000269|PubMed:15532022;Dbxref=dbSNP:rs77718928,PMID:10024431,PMID:15532022 P05062 UniProtKB Natural variant 343 343 . . . ID=VAR_075349;Note=In HFI%3B almost no effect on enzymatic activity at 30 degrees Celsius%2C but reduced activity at higher temperatures. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20848650;Dbxref=dbSNP:rs369586696,PMID:20848650 P05062 UniProtKB Mutagenesis 43 43 . . . Note=Loss of enzymatic activity. Retains the ability to interact with G6PD. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Mutagenesis 46 46 . . . Note=Decreases enzymatic activity. Retains the ability to interact with G6PD. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Mutagenesis 108 108 . . . Note=Decreases enzymatic activity. Retains the ability to interact with G6PD. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Mutagenesis 147 147 . . . Note=Loss of enzymatic activity. Impairs the interaction with G6PD. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Mutagenesis 149 149 . . . Note=Loss of enzymatic activity. Impairs the interaction with G6PD. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Mutagenesis 230 230 . . . Note=Loss of enzymatic activity. Impairs the interaction with G6PD. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Mutagenesis 304 304 . . . Note=Decreases enzymatic activity. Impairs the interaction with G6PD. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35122041;Dbxref=PMID:35122041 P05062 UniProtKB Sequence conflict 54 54 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05062 UniProtKB Sequence conflict 250 250 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05062 UniProtKB Sequence conflict 278 278 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05062 UniProtKB Sequence conflict 309 309 . . . Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05062 UniProtKB Sequence conflict 348 348 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05062 UniProtKB Helix 10 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Turn 25 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XDL P05062 UniProtKB Beta strand 29 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 37 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 53 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 68 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XDM P05062 UniProtKB Helix 94 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 131 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 145 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 161 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Turn 180 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 184 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 199 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 246 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 267 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 277 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XDM P05062 UniProtKB Beta strand 296 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 304 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 308 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 321 338 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Turn 339 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5 P05062 UniProtKB Helix 351 354 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QO5