##gff-version 3 ##sequence-region P0AFI7 1 218 P0AFI7 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7860596;Dbxref=PMID:7860596 P0AFI7 UniProtKB Chain 2 218 . . . ID=PRO_0000167706;Note=Pyridoxine/pyridoxamine 5'-phosphate oxidase P0AFI7 UniProtKB Binding site 14 17 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Binding site 67 72 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903950,ECO:0000269|PubMed:11453690,ECO:0000269|PubMed:15858270;Dbxref=PMID:10903950,PMID:11453690,PMID:15858270 P0AFI7 UniProtKB Binding site 72 72 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11453690;Dbxref=PMID:11453690 P0AFI7 UniProtKB Binding site 82 83 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903950,ECO:0000269|PubMed:11453690,ECO:0000269|PubMed:15858270;Dbxref=PMID:10903950,PMID:11453690,PMID:15858270 P0AFI7 UniProtKB Binding site 88 88 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903950,ECO:0000269|PubMed:11453690,ECO:0000269|PubMed:15858270;Dbxref=PMID:10903950,PMID:11453690,PMID:15858270 P0AFI7 UniProtKB Binding site 89 89 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903950,ECO:0000269|PubMed:11453690,ECO:0000269|PubMed:15858270;Dbxref=PMID:10903950,PMID:11453690,PMID:15858270 P0AFI7 UniProtKB Binding site 111 111 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11786019,ECO:0000269|PubMed:15858270;Dbxref=PMID:11786019,PMID:15858270 P0AFI7 UniProtKB Binding site 129 129 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11453690;Dbxref=PMID:11453690 P0AFI7 UniProtKB Binding site 133 133 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11453690;Dbxref=PMID:11453690 P0AFI7 UniProtKB Binding site 137 137 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11453690;Dbxref=PMID:11453690 P0AFI7 UniProtKB Binding site 146 147 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903950,ECO:0000269|PubMed:11453690,ECO:0000269|PubMed:15858270;Dbxref=PMID:10903950,PMID:11453690,PMID:15858270 P0AFI7 UniProtKB Binding site 191 191 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15858270;Dbxref=PMID:15858270 P0AFI7 UniProtKB Binding site 197 199 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Binding site 201 201 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11786019,ECO:0000269|PubMed:15858270;Dbxref=PMID:11786019,PMID:15858270 P0AFI7 UniProtKB Mutagenesis 14 14 . . . Note=Reduces affinity for substrate about 7-fold%2C but has no effect on catalytic activity. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 14 14 . . . Note=Reduces affinity for substrate about 9-fold%2C but has no effect on catalytic activity. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 17 17 . . . Note=Reduces affinity for substrate 3-fold%2C but has about 5-fold increase in catalytic activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 49 49 . . . Note=Reduces affinity for substrate 3-fold and catalytic activity 2-fold. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 197 197 . . . Note=Reduces affinity for substrate 8000-fold and catalytic activity 16-fold. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 197 197 . . . Note=Reduces affinity for substrate 300-fold and catalytic activity about 4-fold. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 199 199 . . . Note=Reduces affinity for substrate 230-fold%2C but has no effect on catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Mutagenesis 199 199 . . . Note=Reduces catalytic activity about 4-fold%2C but has no effect on affinity for substrate. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786019;Dbxref=PMID:11786019 P0AFI7 UniProtKB Helix 9 12 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JNW P0AFI7 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 31 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 52 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 64 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 78 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 88 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 106 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 110 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 135 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 154 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 167 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G79 P0AFI7 UniProtKB Beta strand 178 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 200 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL P0AFI7 UniProtKB Beta strand 208 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DNL