ID A0A5M9Z1J7_9LACO Unreviewed; 399 AA. AC A0A5M9Z1J7; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 14-DEC-2022, entry version 7. 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 ORFNames=F1C09_07705 {ECO:0000313|EMBL:KAA8812113.1}; OS Lactobacillus crispatus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=47770 {ECO:0000313|EMBL:KAA8812113.1, ECO:0000313|Proteomes:UP000324504}; RN [1] {ECO:0000313|EMBL:KAA8812113.1, ECO:0000313|Proteomes:UP000324504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCK2488 {ECO:0000313|EMBL:KAA8812113.1, RC ECO:0000313|Proteomes:UP000324504}; RA Pan M., Hidalgo-Cantabrana C., Barrangou R.; RT "Comparative analysis of L. crispatus genomes revealed niche specific RT adaptation to different host and body sites."; RL Submitted (SEP-2019) 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; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA8812113.1}. 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; VUAV01000048; KAA8812113.1; -; Genomic_DNA. DR RefSeq; WP_057726928.1; NZ_VUAV01000048.1. DR AlphaFoldDB; A0A5M9Z1J7; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000324504; Unassembled WGS sequence. 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 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 PANTHER; PTHR21060; 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 TIGRFAMs; TIGR00016; ackA; 1. 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}; 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 333..337 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020" FT BINDING 384 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 399 AA; 44049 MW; 2B467FEDBF680959 CRC64; MKKILAINSG SSSFKFKLFT FPDEKVISEG MADRVGLNGS TFTIKVKGEK HQEKVDIPDS ETAVTILLEN LKKYDLIDDP KEIIGIGHRI VAGGEEFKDS TLIDEKSLQK IYDLKQYAPL HNTAEADVIK AFMKVLPGVP EVAVFDTSFH QTLDPVHYLY SLPYKYYEKY GARKYGAHGT SVRYVSQKAA EIMKRDLKDL KLIVCHLGSG ASVTAVKDGK SFDTSMGFSP MAGITMSSRS GDVDPSLLAF VMKKENLDAD QMLKVLNNES GLLGISGISP DMRDLRGDMT KLEGEKKKRA DLARNIFINR IIRYVGAYTL EMRGLDGIAF TAGVGEHDFG VREHVMDSLE LLGLKPDSAA NKENATIITK PNSTIVGMVI PTNEELMIER DVVRVAGLK //