##gff-version 3 P79226 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P79226 UniProtKB Chain 2 364 . . . ID=PRO_0000216942;Note=Fructose-bisphosphate aldolase B P79226 UniProtKB Active site 188 188 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P79226 UniProtKB Active site 230 230 . . . Note=Schiff-base intermediate with dihydroxyacetone-P;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P79226 UniProtKB Binding site 43 43 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P79226 UniProtKB Binding site 272 274 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P79226 UniProtKB Binding site 304 304 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00883 P79226 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 P79226 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P79226 UniProtKB Modified residue 13 13 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P79226 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 39 39 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 119 119 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 121 121 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P79226 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00884 P79226 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00884 P79226 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05062 P79226 UniProtKB Modified residue 317 317 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91Y97 P79226 UniProtKB Helix 10 24 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 25 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 29 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 37 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 53 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 68 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 81 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 94 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 131 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 145 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 161 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 184 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 199 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 246 258 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 267 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 277 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 296 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 304 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Helix 321 338 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Turn 339 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ P79226 UniProtKB Beta strand 353 357 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FDJ