ID A8FG71_BACP2 Unreviewed; 394 AA. AC A8FG71; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 112. DE RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=BPUM_2579 {ECO:0000313|EMBL:ABV63238.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV63238.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV63238.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63238.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). RN [2] {ECO:0000313|EMBL:ABV63238.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63238.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23812891; DOI=10.1007/s00792-013-0559-z; RA Tirumalai M.R., Fox G.E.; RT "An ICEBs1-like element may be associated with the extreme radiation and RT desiccation resistance of Bacillus pumilus SAFR-032 spores."; RL Extremophiles 17:767-774(2013). RN [3] {ECO:0000313|EMBL:ABV63238.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63238.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23799069; RA Tirumalai M.R., Rastogi R., Zamani N., O'Bryant Williams E., Allen S., RA Diouf F., Kwende S., Weinstock G.M., Venkateswaran K.J., Fox G.E.; RT "Candidate genes that may be responsible for the unusual resistances RT exhibited by Bacillus pumilus SAFR-032 spores."; RL PLoS ONE 8:E66012-E66012(2013). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and CC ATP. Can also catalyze the reverse reaction. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00020}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; CC acetyl-CoA from acetate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SIMILARITY: Belongs to the acetokinase family. CC {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00020, CC ECO:0000256|RuleBase:RU003835}. 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; CP000813; ABV63238.1; -; Genomic_DNA. DR RefSeq; WP_003216471.1; NC_009848.4. DR AlphaFoldDB; A8FG71; -. DR STRING; 315750.BPUM_2579; -. DR PaxDb; 315750-BPUM_2579; -. DR GeneID; 5621844; -. DR KEGG; bpu:BPUM_2579; -. DR eggNOG; COG0282; Bacteria. DR HOGENOM; CLU_020352_0_1_9; -. DR OrthoDB; 9802453at2; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000001355; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00020}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00020}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00020}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00020}; Reference proteome {ECO:0000313|Proteomes:UP000001355}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00020}. FT ACT_SITE 146 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 206..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 281..283 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 329..333 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 382 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT SITE 178 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT SITE 239 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" SQ SEQUENCE 394 AA; 43179 MW; 28B095AD23DEFC90 CRC64; MSKIIAINAG SSSLKFQLFD MPEETVLTKG LVERIGMDNS IFTISVDGEK KTEVTDIPDH AVAVKMLLEK LIEFNIIKDF NEIDGVGHRV VHGGEKFSDS VLLTDEVIND IDQLSELAPL HNPANVVGIK AFKQILPDVP AIAVFDTAFH QTMPEQSYLY SLPYDYYKNF GIRKYGFHGT SHKFVTERAS ELLGRPLEEL RLISCHLGNG ASIAAVEGGR SIDTSMGFTP LAGVAMGTRS GNIDPALIPF IMEKTGHTAE EVLSTLNKKS GLLGVSGLSS DLRDIEEATE EGNDRAEVAL DIFASRIHKY IGSYAARMNG VDAIIFTAGI GENSSEVRAR VLRGLEFMGV YWDPSLNNMR GEEAFISYPH SPVKVIVIPT NEEVMIARDV MRLA //