##gff-version 3 P0A825 UniProtKB Chain 1 417 . . . ID=PRO_0000113573;Note=Serine hydroxymethyltransferase P0A825 UniProtKB Binding site 35 35 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 55 55 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 65 65 . . . Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0007744|PDB:1DFO;Dbxref=PMID:10656824 P0A825 UniProtKB Binding site 99 99 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 121 121 . . . Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000255|HAMAP-Rule:MF_00051,ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 125 127 . . . Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000255|HAMAP-Rule:MF_00051,ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 175 175 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 203 203 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 228 228 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19883126,ECO:0007744|PDB:3G8M;Dbxref=PMID:19883126 P0A825 UniProtKB Binding site 235 235 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19883126,ECO:0007744|PDB:3G8M;Dbxref=PMID:19883126 P0A825 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 263 263 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 355 357 . . . Ontology_term=ECO:0000255,ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000255|HAMAP-Rule:MF_00051,ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Binding site 363 363 . . . Ontology_term=ECO:0000305,ECO:0000305,ECO:0007744,ECO:0007744;evidence=ECO:0000305|PubMed:10656824,ECO:0000305|PubMed:10858298,ECO:0007744|PDB:1DFO,ECO:0007744|PDB:1EQB;Dbxref=PMID:10656824,PMID:10858298 P0A825 UniProtKB Site 55 55 . . . Note=Transaldimination and stability P0A825 UniProtKB Site 228 228 . . . Note=Plays an important role in substrate specificity;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_00051,ECO:0000269|PubMed:1517215;Dbxref=PMID:1517215 P0A825 UniProtKB Site 235 235 . . . Note=Transaldimination and stability P0A825 UniProtKB Modified residue 54 54 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842 P0A825 UniProtKB Modified residue 62 62 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 229 229 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|HAMAP-Rule:MF_00051,ECO:0000269|PubMed:19883126,ECO:0007744|PDB:3G8M;Dbxref=PMID:19883126 P0A825 UniProtKB Modified residue 242 242 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 250 250 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842 P0A825 UniProtKB Modified residue 250 250 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 277 277 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 285 285 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842 P0A825 UniProtKB Modified residue 293 293 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 331 331 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 346 346 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 354 354 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842 P0A825 UniProtKB Modified residue 354 354 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151122;Dbxref=PMID:21151122 P0A825 UniProtKB Modified residue 375 375 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842 P0A825 UniProtKB Mutagenesis 55 55 . . . Note=50 and 15-fold increase in the affinity for serine and tetrahydrofolate%2C respectively%2C and 4-fold decrease in the catalytic efficiency. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19883126;Dbxref=PMID:19883126 P0A825 UniProtKB Mutagenesis 65 65 . . . Note=Decrease in catalytic activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10858298;Dbxref=PMID:10858298 P0A825 UniProtKB Mutagenesis 85 85 . . . Note=Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state%3B when associated with A-276. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19019081;Dbxref=PMID:19019081 P0A825 UniProtKB Mutagenesis 214 214 . . . Note=No significant difference in catalytic efficiency and affinity compared to the wild-type. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 214 214 . . . Note=No significant difference in catalytic efficiency and affinity compared to the wild-type. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 216 216 . . . Note=No significant difference in catalytic efficiency and affinity compared to the wild-type. Alteration in the folding rate. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 216 216 . . . Note=Important decrease in affinity and catalytic efficiency. Severely compromised in folding into a catalytically competent enzyme. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 218 218 . . . Note=No significant difference in catalytic efficiency and affinity compared to the wild-type. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 218 218 . . . Note=No significant difference in catalytic efficiency and affinity compared to the wild-type. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 228 228 . . . Note=Utilize substrates and substrate analogs more effectively for a variety of alternate non-physiological reactions. H->D%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1517215;Dbxref=PMID:1517215 P0A825 UniProtKB Mutagenesis 235 235 . . . Note=1500- and 20-fold increase in the affinity for serine and tetrahydrofolate%2C respectively%2C and 15-fold decrease in the catalytic efficiency. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19883126;Dbxref=PMID:19883126 P0A825 UniProtKB Mutagenesis 235 235 . . . Note=450- and 11-fold increase in the affinity for serine and tetrahydrofolate%2C respectively%2C and 60-fold decrease in the catalytic efficiency. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19883126;Dbxref=PMID:19883126 P0A825 UniProtKB Mutagenesis 235 235 . . . Note=900- and 17-fold increase in the affinity for serine and tetrahydrofolate%2C respectively%2C and 30-fold decrease in the catalytic efficiency. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19883126;Dbxref=PMID:19883126 P0A825 UniProtKB Mutagenesis 258 258 . . . Note=Important decrease in affinity and catalytic efficiency. Reduced thermal stability. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 258 258 . . . Note=Important decrease in affinity and catalytic efficiency. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 264 264 . . . Note=Important decrease in affinity and catalytic efficiency. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 264 264 . . . Note=Important decrease in affinity and catalytic efficiency. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773539;Dbxref=PMID:12773539 P0A825 UniProtKB Mutagenesis 276 276 . . . Note=Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state%3B when associated with A-85. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19019081;Dbxref=PMID:19019081 P0A825 UniProtKB Mutagenesis 363 363 . . . Note=It does not bind serine and glycine and shows no activity with serine as the substrate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7925461;Dbxref=PMID:7925461 P0A825 UniProtKB Mutagenesis 363 363 . . . Note=Exhibits only 0.03%25 of the catalytic activity of the wild-type and a 15-fold reduction in affinity for glycine and serine. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7925461;Dbxref=PMID:7925461 P0A825 UniProtKB Mutagenesis 372 372 . . . Note=No significant difference compared to the wild-type. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7925461;Dbxref=PMID:7925461 P0A825 UniProtKB Mutagenesis 372 372 . . . Note=No significant difference compared to the wild-type. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7925461;Dbxref=PMID:7925461 P0A825 UniProtKB Helix 8 11 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 13 28 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 41 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 50 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 62 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 69 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 89 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 98 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 115 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Turn 121 124 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 135 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 149 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 155 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 168 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 183 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 196 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 205 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Turn 217 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 220 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 237 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 246 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Turn 257 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 266 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 282 304 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 310 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 315 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 324 326 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 330 339 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Turn 356 358 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 360 365 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 367 371 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 376 391 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Turn 392 394 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Helix 396 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO P0A825 UniProtKB Beta strand 415 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DFO