ID ACKA_BUCAP Reviewed; 403 AA. AC Q8K9W6; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 107. 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=BUsg_169; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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; AE013218; AAM67736.1; -; Genomic_DNA. DR AlphaFoldDB; Q8K9W6; -. DR SMR; Q8K9W6; -. DR STRING; 198804.BUsg_169; -. DR KEGG; bas:BUsg_169; -. DR eggNOG; COG0282; Bacteria. DR HOGENOM; CLU_020352_0_1_6; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; 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:SF19; ACETATE 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; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Transferase. FT CHAIN 1..403 FT /note="Acetate kinase" FT /id="PRO_0000107539" FT ACT_SITE 153 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 213..217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 288..290 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 336..340 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 390 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 185 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 246 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" SQ SEQUENCE 403 AA; 45211 MW; 408D7ABED18A8FA5 CRC64; MVKILNNLIF VLNCGSSSVK FAILNPDNKK KYLSGLVECL FLSKTYMKWK DLTTEHKKCI GSNLSHKDAL NFIFNKFFLE KKDIYKNIVG IGHRVVHGGN KIKSSTLIDD NIIQLIQKAI SFAPLHNPAN LIGIKTAIEK FPIFAKKNVA VFDTSFYQNM PETSFLYAIP YFFYKEHHIR RYGAHGTSHH YVASEVALIL NKNFNSLNVI TCHLGNGASV SAVCNGICVD TSMGLTPLEG LVMGTRSGDI DPSIIFFMYQ KLGMSIDEIH TILTKESGLL GLSGISSDFR YFEKKYYFEK KARLAVDIFC HRLSKYIASY MSLMENNLDA IVFTGGIGEN VPLIREITLS KLLLIGFKID TQRNLGIKNG KHGLITTDKS RPAFVIPTDE ELAIAQETIK IIK //