ID ACKA_DICT6 Reviewed; 399 AA. AC B5YDP7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 02-SEP-2026, entry version 88. DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=DICTH_0789; OS Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12). OC Bacteria; Pseudomonadati; Dictyoglomota; Dictyoglomia; Dictyoglomales; OC Dictyoglomaceae; Dictyoglomus. OX NCBI_TaxID=309799; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35947 / DSM 3960 / H-6-12; RX PubMed=24558247; DOI=10.1128/genomea.00109-14; RA Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N., RA Ward N., Robb F.T., Eisen J.A.; RT "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus RT thermophilum H-6-12."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and CC ATP. Can also catalyze the reverse reaction. {ECO:0000255|HAMAP- CC Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352, CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00020}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; CC acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00020}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001146; ACI18400.1; -; Genomic_DNA. DR RefSeq; WP_012547032.1; NC_011297.1. DR AlphaFoldDB; B5YDP7; -. DR SMR; B5YDP7; -. DR STRING; 309799.DICTH_0789; -. DR PaxDb; 309799-DICTH_0789; -. DR KEGG; dth:DICTH_0789; -. DR eggNOG; COG0282; Bacteria. DR HOGENOM; CLU_020352_0_1_0; -. DR OrthoDB; 9802453at2; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000001733; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006083; P:acetate metabolic process; IEA:TreeGrafter. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd24010; ASKHA_NBD_AcK_PK; 1. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_00020; Acetate_kinase; 1. DR InterPro; IPR004372; Ac/propionate_kinase. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. DR InterPro; IPR043129; ATPase_NBD. DR NCBIfam; TIGR00016; ackA; 1. DR PANTHER; PTHR21060; ACETATE KINASE; 1. DR PANTHER; PTHR21060:SF15; ACETATE KINASE-RELATED; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..399 FT /note="Acetate kinase" FT /id="PRO_1000089971" FT ACT_SITE 148 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 91 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 208..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 283..285 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 384 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 180 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 241 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" SQ SEQUENCE 399 AA; 44258 MW; DFBF2078C1B036EB CRC64; MKVLVLNCGS SSVKYQVFDM KDEKVLAKGL AERIGLDGSR IVYQRGVESK KVFEIPLPTH KKAIEEIFRL LVDKNDGILS SLNEIDAVGH RVVHGGDKFI ESVLVNDEVY NTFKGILDLA PLHNPYNLQG VDACLELMPG VPQVLVFDTS FHQTMPEEAY IYALPYEWYE KYKIRRYGFH GTSHYYVSRR VAELIGRPVE ELKIISCHLG NGASITAIKN GKSIDTSMGY TPLEGLVMGT RCGDIDPAIP ILLMEKENLS PKQIDEILNK KSGILGISGV SSDFRDVGEA AEKGNKRAEL ALKVFAYRVK KYIGAYHAIL GGLDVLVFTA GVGERGPLER SLICSGLEHL GIKLDPEKNK VKGEELKIST PDSKVEVWVI PTNEELMIAR ETVRVVGKK //