ID ACKA_METTE Reviewed; 408 AA. AC P38502; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 122. 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}; Synonyms=ack; OS Methanosarcina thermophila. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2210; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1; RX PubMed=8226623; DOI=10.1128/jb.175.21.6822-6829.1993; RA Latimer M.T., Ferry J.G.; RT "Cloning, sequence analysis, and hyperexpression of the genes encoding RT phosphotransacetylase and acetate kinase from Methanosarcina thermophila."; RL J. Bacteriol. 175:6822-6829(1993). RN [2] RP PROTEIN SEQUENCE OF 1-17, CATALYTIC ACTIVITY, SUBUNIT, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2844814; DOI=10.1016/s0021-9258(19)37608-2; RA Aceti D.J., Ferry J.G.; RT "Purification and characterization of acetate kinase from acetate-grown RT Methanosarcina thermophila. Evidence for regulation of synthesis."; RL J. Biol. Chem. 263:15444-15448(1988). RN [3] RP CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND MUTAGENESIS OF ASN-7; SER-10; RP SER-12; LYS-14; ASP-148; ASN-211 AND GLU-384. RX PubMed=11562377; DOI=10.1074/jbc.m108355200; RA Miles R.D., Iyer P.P., Ferry J.G.; RT "Site-directed mutational analysis of active site residues in the acetate RT kinase from Methanosarcina thermophila."; RL J. Biol. Chem. 276:45059-45064(2001). RN [4] RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF VAL-93; LEU-122; PHE-179 AND PRO-232. RX PubMed=15774882; DOI=10.1128/jb.187.7.2386-2394.2005; RA Ingram-Smith C., Gorrell A., Lawrence S.H., Iyer P., Smith K., Ferry J.G.; RT "Characterization of the acetate binding pocket in the Methanosarcina RT thermophila acetate kinase."; RL J. Bacteriol. 187:2386-2394(2005). RN [5] RP CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS RP OF ARG-91 AND ARG-241. RX PubMed=17999468; DOI=10.1021/bi701292a; RA Gorrell A., Ferry J.G.; RT "Investigation of the Methanosarcina thermophila acetate kinase mechanism RT by fluorescence quenching."; RL Biochemistry 46:14170-14176(2007). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH THE ATP ANALOG ADP, RP ACTIVE SITE, AND SUBUNIT. RX PubMed=11133963; DOI=10.1128/jb.183.2.680-686.2001; RA Buss K.A., Cooper D.R., Ingram-Smith C., Ferry J.G., Sanders D.A., RA Hasson M.S.; RT "Urkinase: structure of acetate kinase, a member of the ASKHA superfamily RT of phosphotransferases."; RL J. Bacteriol. 183:680-686(2001). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-399 IN COMPLEX WITH THE ATP RP ANALOGS ADP; AMP; ALF3 AND THE SUBSTRATE ACETATE, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, ACTIVITY REGULATION, COFACTOR, RP SUBUNIT, AND MUTAGENESIS OF ARG-91 AND ARG-241. RX PubMed=15647264; DOI=10.1074/jbc.m412118200; RA Gorrell A., Lawrence S.H., Ferry J.G.; RT "Structural and kinetic analyses of arginine residues in the active site of RT the acetate kinase from Methanosarcina thermophila."; RL J. Biol. Chem. 280:10731-10742(2005). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and CC ATP. Can also catalyze the reverse reaction. Can also phosphorylate CC propionate, but has very low activity toward butyrate. CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:15774882}. 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, ECO:0000269|PubMed:11562377, CC ECO:0000269|PubMed:15647264, ECO:0000269|PubMed:15774882, CC ECO:0000269|PubMed:17999468, ECO:0000269|PubMed:2844814, CC ECO:0000269|PubMed:8226623}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00020, ECO:0000269|PubMed:11562377, CC ECO:0000269|PubMed:15647264}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00020, ECO:0000269|PubMed:11562377, CC ECO:0000269|PubMed:15647264}; CC Note=Mg(2+). Can also accept Mn(2+). The Mg(2+) is bound between two CC conserved protein residues and the ATP phosphate groups. CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:11562377, CC ECO:0000269|PubMed:15647264}; CC -!- ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate, hydroxylamine CC and phenylglyoxal. {ECO:0000269|PubMed:15647264, CC ECO:0000269|PubMed:8226623}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=71 uM for ATP {ECO:0000269|PubMed:15647264, CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468, CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623}; CC KM=98 uM for ADP {ECO:0000269|PubMed:15647264, CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468, CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623}; CC KM=1.5 mM for acetate {ECO:0000269|PubMed:15647264, CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468, CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623}; CC KM=0.47 mM for acetyl phosphate {ECO:0000269|PubMed:15647264, CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468, CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623}; CC Temperature dependence: CC Optimum temperature is 65 degrees Celsius. Protected from thermal CC inactivation by ATP. {ECO:0000269|PubMed:15647264, CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468, CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623}; 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 ECO:0000269|PubMed:11133963, ECO:0000269|PubMed:11562377, CC ECO:0000269|PubMed:15647264, ECO:0000269|PubMed:17999468, CC ECO:0000269|PubMed:2844814}. 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; L23147; AAA72042.1; -; Unassigned_DNA. DR PIR; B49338; B49338. DR PDB; 1G99; X-ray; 2.50 A; A/B=1-408. DR PDB; 1TUU; X-ray; 2.50 A; A/B=1-399. DR PDB; 1TUY; X-ray; 3.00 A; A/B=1-399. DR PDBsum; 1G99; -. DR PDBsum; 1TUU; -. DR PDBsum; 1TUY; -. DR AlphaFoldDB; P38502; -. DR SMR; P38502; -. DR KEGG; ag:AAA72042; -. DR BRENDA; 2.7.2.1; 3281. DR SABIO-RK; P38502; -. DR UniPathway; UPA00340; UER00458. DR EvolutionaryTrace; P38502; -. 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; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Transferase. FT CHAIN 1..408 FT /note="Acetate kinase" FT /id="PRO_0000107650" FT ACT_SITE 148 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020, FT ECO:0000269|PubMed:11133963, ECO:0000269|PubMed:15647264" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 91 FT /ligand="substrate" FT BINDING 208..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 283..285 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 331..335 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 384 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305" FT SITE 180 FT /note="Transition state stabilizer" FT SITE 241 FT /note="Transition state stabilizer" FT MUTAGEN 7 FT /note="N->A: Almost abolishes catalytic activity. Requires FT increased magnesium levels for activity. Strongly decreases FT affinity for acetate." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 7 FT /note="N->D: Almost abolishes catalytic activity. Strongly FT decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 10 FT /note="S->A,T: Strongly decreases catalytic activity. FT Strongly decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 11 FT /note="S->A: Decreases catalytic activity. Decreases FT affinity for acetate." FT MUTAGEN 11 FT /note="S->T: Strongly decreases catalytic activity. FT Strongly decreases affinity for acetate." FT MUTAGEN 12 FT /note="S->A: Decreases catalytic activity. Strongly FT decreases affinity for acetate. Requires increased FT magnesium levels for enzyme activity." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 12 FT /note="S->T: Decreases catalytic activity. Strongly FT decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 14 FT /note="K->A: Strongly decreases enzyme activity." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 14 FT /note="K->R: Reduces enzyme activity." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 91 FT /note="R->A,L: Decreases catalytic activity. Decreases FT affinity for acetate." FT /evidence="ECO:0000269|PubMed:15647264, FT ECO:0000269|PubMed:17999468" FT MUTAGEN 93 FT /note="V->A: Decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:15774882" FT MUTAGEN 122 FT /note="L->A: Decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:15774882" FT MUTAGEN 148 FT /note="D->A,E,N: Abolishes catalytic activity. Decreases FT affinity for acetate, but not for ATP." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 179 FT /note="F->A: Decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:15774882" FT MUTAGEN 211 FT /note="N->A: Slightly reduced enzyme activity." FT /evidence="ECO:0000269|PubMed:11562377" FT MUTAGEN 232 FT /note="P->A: Decreases affinity for acetate." FT /evidence="ECO:0000269|PubMed:15774882" FT MUTAGEN 241 FT /note="R->K,L: Decreases catalytic activity. Strongly FT reduced affinity for ATP." FT /evidence="ECO:0000269|PubMed:15647264, FT ECO:0000269|PubMed:17999468" FT MUTAGEN 384 FT /note="E->A: Almost abolishes catalytic activity. Strongly FT decreases affinity for acetate. Requires strongly increased FT magnesium levels for enzyme activity." FT /evidence="ECO:0000269|PubMed:11562377" FT STRAND 2..8 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 13..19 FT /evidence="ECO:0007829|PDB:1G99" FT TURN 20..23 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 24..33 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 60..71 FT /evidence="ECO:0007829|PDB:1G99" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:1G99" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 107..115 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:1G99" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 124..137 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 143..147 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 150..154 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 166..172 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 181..195 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 203..219 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 249..257 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 261..270 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 273..278 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 284..292 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 296..319 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 324..329 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 330..335 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 337..344 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:1G99" FT STRAND 374..379 FT /evidence="ECO:0007829|PDB:1G99" FT HELIX 384..397 FT /evidence="ECO:0007829|PDB:1G99" SQ SEQUENCE 408 AA; 44337 MW; 1A484DF8A7258800 CRC64; MKVLVINAGS SSLKYQLIDM TNESALAVGL CERIGIDNSI ITQKKFDGKK LEKLTDLPTH KDALEEVVKA LTDDEFGVIK DMGEINAVGH RVVHGGEKFT TSALYDEGVE KAIKDCFELA PLHNPPNMMG ISACAEIMPG TPMVIVFDTA FHQTMPPYAY MYALPYDLYE KHGVRKYGFH GTSHKYVAER AALMLGKPAE ETKIITCHLG NGSSITAVEG GKSVETSMGF TPLEGLAMGT RCGSIDPAIV PFLMEKEGLT TREIDTLMNK KSGVLGVSGL SNDFRDLDEA ASKGNRKAEL ALEIFAYKVK KFIGEYSAVL NGADAVVFTA GIGENSASIR KRILTGLDGI GIKIDDEKNK IRGQEIDIST PDAKVRVFVI PTNEELAIAR ETKEIVETEV KLRSSIPV //