ID A1B9S8_PARDP Unreviewed; 367 AA. AC A1B9S8; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 111. 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=Pden_4208 {ECO:0000313|EMBL:ABL72272.1}; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Paracoccus. OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72272.1, ECO:0000313|Proteomes:UP000000361}; RN [1] {ECO:0000313|Proteomes:UP000000361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., RA Richardson P.; RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000490; ABL72272.1; -; Genomic_DNA. DR RefSeq; WP_011750437.1; NC_008687.1. DR AlphaFoldDB; A1B9S8; -. DR STRING; 318586.Pden_4208; -. DR EnsemblBacteria; ABL72272; ABL72272; Pden_4208. DR GeneID; 75503591; -. DR KEGG; pde:Pden_4208; -. DR eggNOG; COG0282; Bacteria. DR HOGENOM; CLU_020352_0_0_5; -. DR OrthoDB; 9802453at2; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000361; Chromosome 2. 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:SF15; PROPIONATE KINASE PDUW; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 2. 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}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000000361}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00020}. FT ACT_SITE 145 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 203..207 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 323..327 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 354 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT SITE 176 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT SITE 236 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" SQ SEQUENCE 367 AA; 38600 MW; D30649F83C9EAF00 CRC64; MIAAILTLNA GSSSLKFRVF AREGLALLAR GAVSRIGADA ELVAELTGAS QVRSPVAGGD HAAAMQAVLD FIDAHDEGWR IEAVAHRIVH GGTRYTRSTP VTPQVLVDLA ALIPLAPLHQ PHGLAAIAAA RRLVGEDVPN LACFDTAFHA GRDALFTHFA LPEPLFEQGV RRYGFHGLSY QWLAQVLARD HPELHRGRVV AAHLGNGASL CAMHQGRSVD TTMGMTAVDG IPMGTRSGAV DPGAILLMQR SFGMTPEEIE DLIYNRSGLL GMSGRSNDVA ALLTDGSAQS RFALDFFALR CAQAAAAMAV SLGGIDAMVF TGGIGENAAP VREAILRHMA PLGDFATLVI PANEECMMAM EAAALLA //