ID ACKA_BUCBP Reviewed; 400 AA. AC Q89AS8; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 1. DT 02-SEP-2026, entry version 114. 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=bbp_164; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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; AE016826; AAO26897.1; -; Genomic_DNA. DR RefSeq; WP_011091298.1; NC_004545.1. DR AlphaFoldDB; Q89AS8; -. DR SMR; Q89AS8; -. DR STRING; 224915.bbp_164; -. DR KEGG; bab:bbp_164; -. DR eggNOG; COG0282; Bacteria. DR HOGENOM; CLU_020352_0_1_6; -. DR OrthoDB; 9802453at2; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 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:SF17; PROPIONATE KINASE; 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..400 FT /note="Acetate kinase" FT /id="PRO_0000107540" FT ACT_SITE 150 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 17 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 210..214 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 285..287 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 333..337 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 387 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 182 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 243 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" SQ SEQUENCE 400 AA; 44388 MW; DB7644AE6A79DC1C CRC64; MFNKLVLILN CGSSSLKFSV VSSDNYTTKL SGIVEFLNLS QIRFFWKIKK KEYVRVINKS KSYDYALNYI LTKILKEESK IFNNIACVGH RVVHGGVNLN KSVLITQEII KLITDACSFA PLHNPINLLG IKASHAVLPH LKEKNVAVFD TSFHSSIPKF AYLYAIPYKF YKKFGIRKYG AHGISCQYSV CRSSELLQIE LTSLNIIICH LGGGASVSVV KNGVCVDTSM GLTPLEGLIM GTRSGDIDPS VIFFMNKQLN LSISTINNIL INKSGLLGLS GVSSDFRNLE SEYNSNIRIK LAIDMFCYRL SKYISGYMSV VKGKLHGIVF TGGIGENSSL VRSIVISKLA FLNFKLNSDI NMLMKSGKEG FINIKNTFPI LVIPANEELI IAKESFSEIN //