ID ACKA_CLAM3 Reviewed; 396 AA. AC A5CPD5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 02-SEP-2026, entry version 95. 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=CMM_0896; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Microbacteriaceae; Clavibacter. OX NCBI_TaxID=443906; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382; RX PubMed=18192381; DOI=10.1128/jb.01595-07; RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C., RA Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., RA Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved RT in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). 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; AM711867; CAN00933.1; -; Genomic_DNA. DR RefSeq; WP_012037581.1; NC_009480.1. DR AlphaFoldDB; A5CPD5; -. DR SMR; A5CPD5; -. DR KEGG; cmi:CMM_0896; -. DR eggNOG; COG0282; Bacteria. DR HOGENOM; CLU_020352_0_1_11; -. DR OrthoDB; 9802453at2; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000001564; 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..396 FT /note="Acetate kinase" FT /id="PRO_1000002219" FT ACT_SITE 146 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 206..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 280..282 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 328..332 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT BINDING 382 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 178 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" FT SITE 239 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020" SQ SEQUENCE 396 AA; 41946 MW; 7B829C994887C382 CRC64; MPVVLVVNSG SSSFKYQLIE MDTESVLASG LVERIGEPTG STRHKAGGDS WERELPIADH TAGFQAMLDA FAEHGPSLEE EPPVAVGHRV VHGGDVFVEP TVVTDDVKAD IDDLSALAPL HNPGALQGIA AAQTAFPDVP HVAVFDTAFH QTLPAEAYTY AIDRELAAAH RIRRYGFHGT SHKFVSEAAA RLLGKPLEET RIIVLHLGNG ASAAAVQGGR SIDTSMGLTP LEGLVMGTRS GDIDPAILFH LARHTDLGLD DLETLLNRRS GLLGLTGLGD MRDVQRAAAD GDEAAQTALG VYRHRIRHYV GAYAAQLGGV DAVVFTAGVG ENNPLVRRRS LAGLEFMGIG IDDDRNELIS SEARFVSPEG SPVAVLVIPT DEELEIARQS LAATAG //