##gff-version 3 P38502 UniProtKB Chain 1 408 . . . ID=PRO_0000107650;Note=Acetate kinase P38502 UniProtKB Active site 148 148 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_00020,ECO:0000269|PubMed:11133963,ECO:0000269|PubMed:15647264;Dbxref=PMID:11133963,PMID:15647264 P38502 UniProtKB Binding site 7 7 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P38502 UniProtKB Binding site 14 14 . . . . P38502 UniProtKB Binding site 91 91 . . . . P38502 UniProtKB Binding site 208 212 . . . . P38502 UniProtKB Binding site 283 285 . . . . P38502 UniProtKB Binding site 331 335 . . . . P38502 UniProtKB Binding site 384 384 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P38502 UniProtKB Site 180 180 . . . Note=Transition state stabilizer P38502 UniProtKB Site 241 241 . . . Note=Transition state stabilizer P38502 UniProtKB Mutagenesis 7 7 . . . Note=Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 7 7 . . . Note=Almost abolishes catalytic activity. Strongly decreases affinity for acetate. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 10 10 . . . Note=Strongly decreases catalytic activity. Strongly decreases affinity for acetate. S->A%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 11 11 . . . Note=Decreases catalytic activity. Decreases affinity for acetate. S->A P38502 UniProtKB Mutagenesis 11 11 . . . Note=Strongly decreases catalytic activity. Strongly decreases affinity for acetate. S->T P38502 UniProtKB Mutagenesis 12 12 . . . Note=Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 12 12 . . . Note=Decreases catalytic activity. Strongly decreases affinity for acetate. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 14 14 . . . Note=Strongly decreases enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 14 14 . . . Note=Reduces enzyme activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 91 91 . . . Note=Decreases catalytic activity. Decreases affinity for acetate. R->A%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15647264,ECO:0000269|PubMed:17999468;Dbxref=PMID:15647264,PMID:17999468 P38502 UniProtKB Mutagenesis 93 93 . . . Note=Decreases affinity for acetate. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15774882;Dbxref=PMID:15774882 P38502 UniProtKB Mutagenesis 122 122 . . . Note=Decreases affinity for acetate. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15774882;Dbxref=PMID:15774882 P38502 UniProtKB Mutagenesis 148 148 . . . Note=Abolishes catalytic activity. Decreases affinity for acetate%2C but not for ATP. D->A%2CE%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 179 179 . . . Note=Decreases affinity for acetate. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15774882;Dbxref=PMID:15774882 P38502 UniProtKB Mutagenesis 211 211 . . . Note=Slightly reduced enzyme activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Mutagenesis 232 232 . . . Note=Decreases affinity for acetate. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15774882;Dbxref=PMID:15774882 P38502 UniProtKB Mutagenesis 241 241 . . . Note=Decreases catalytic activity. Strongly reduced affinity for ATP. R->K%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15647264,ECO:0000269|PubMed:17999468;Dbxref=PMID:15647264,PMID:17999468 P38502 UniProtKB Mutagenesis 384 384 . . . Note=Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11562377;Dbxref=PMID:11562377 P38502 UniProtKB Beta strand 2 8 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Turn 20 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 24 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 60 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 87 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Turn 96 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 107 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 124 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 150 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 157 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 166 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 181 195 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 203 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 222 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 249 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 261 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 273 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 284 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 296 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 324 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 330 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 337 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 348 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 358 360 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Beta strand 374 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99 P38502 UniProtKB Helix 384 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G99