##gff-version 3 P9WIL5 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11669627,ECO:0007744|PubMed:21969609;Dbxref=PMID:11669627,PMID:21969609 P9WIL5 UniProtKB Chain 2 309 . . . ID=PRO_0000128245;Note=Pantothenate synthetase P9WIL5 UniProtKB Active site 47 47 . . . Note=Proton donor P9WIL5 UniProtKB Binding site 40 47 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16460002;Dbxref=PMID:16460002 P9WIL5 UniProtKB Binding site 72 72 . . . . P9WIL5 UniProtKB Binding site 72 72 . . . . P9WIL5 UniProtKB Binding site 88 88 . . . . P9WIL5 UniProtKB Binding site 89 89 . . . . P9WIL5 UniProtKB Binding site 92 92 . . . . P9WIL5 UniProtKB Binding site 158 161 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16460002;Dbxref=PMID:16460002 P9WIL5 UniProtKB Binding site 164 164 . . . . P9WIL5 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16460002;Dbxref=PMID:16460002 P9WIL5 UniProtKB Binding site 195 198 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16460002;Dbxref=PMID:16460002 P9WIL5 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21969609;Dbxref=PMID:21969609 P9WIL5 UniProtKB Mutagenesis 44 44 . . . Note=More than 1000-fold reduction in activity and 52-fold decrease in adenylate formation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Mutagenesis 47 47 . . . Note=More than 1000-fold reduction in activity and 60-fold decrease in adenylate formation. 10-fold decrease in the affinity for ATP. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Mutagenesis 69 69 . . . Note=More than 1000-fold reduction in activity and 50-fold decrease in adenylate formation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Mutagenesis 72 72 . . . Note=More than 1000-fold reduction in activity and 45-fold decrease in adenylate formation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Mutagenesis 77 77 . . . Note=No effect. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12717031;Dbxref=PMID:12717031 P9WIL5 UniProtKB Mutagenesis 160 160 . . . Note=More than 1000-fold reduction in activity and 50-fold decrease in the affinity for ATP. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Mutagenesis 160 160 . . . Note=More than 1000-fold reduction in activity and 120-fold decrease in adenylate formation. The enzymatic activity and the affinity for beta-alanine can be increased 10- and 3-fold%2C respectively%2C by alkylation of cysteine of mutant C-160. K->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Mutagenesis 164 164 . . . Note=50-fold reduction in activity and slight reduction in the affinity for beta-alanine. 30- and 40-fold decrease in adenylate formation and pantothenate formation%2C respectively. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15170354;Dbxref=PMID:15170354 P9WIL5 UniProtKB Beta strand 12 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 17 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 33 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 45 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 60 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 70 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 78 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 86 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 106 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 116 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 135 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1MOP P9WIL5 UniProtKB Helix 162 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 204 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 212 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 228 240 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 246 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 258 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 264 274 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Beta strand 277 286 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3COV P9WIL5 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3IVC P9WIL5 UniProtKB Beta strand 294 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3IVC