ID   ACKA_METMZ              Reviewed;         408 AA.
AC   P0CW04; Q8PZJ7; Q8X269;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 38.
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 mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2-P;
RA   Tonouti A., Tohyama H., Nishizaki Y.;
RT   "Acetate kinase encoding (ack) gene of Methanosarcina mazei 2-P strain
RT   isolated from a Japanese paddy field soil.";
RL   Submitted (SEP-2001) 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: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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; AB071281; BAB71961.2; -; Genomic_DNA.
DR   AlphaFoldDB; P0CW04; -.
DR   SMR; P0CW04; -.
DR   BRENDA; 2.7.2.1; 3270.
DR   UniPathway; UPA00340; UER00458.
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; PTHR21060; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; SSF53067; 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; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..408
FT                   /note="Acetate kinase"
FT                   /id="PRO_0000107649"
FT   ACT_SITE        148
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         208..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         283..285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         331..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         384
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   SITE            180
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   SITE            241
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   408 AA;  44468 MW;  6D9AED9F43144668 CRC64;
     MKVLVINAGS SSLKYQLIDM TNESALAIGL CERIGIDNSI ITQKRFDGKK LEKQTDLPNH
     KIALEEVVKA LTDSEFGVIK SMDEINAVGH RVVHGGEKFN SSALINEGVE QAIKDCFELA
     PLHNPPNMMG ISSCQEIMPG VPMVAVFDTA FHHTIPPYAY MYALPYELYE KYGIRKYGFH
     GTSHFYVAKR AAAMLGKPEQ DVKVITCHLG NGSSITAVKG GKSIETTMGF TPLEGVAMGT
     RCGSIDPAVV PFIMEKEGLS TREIDTLMNK KSGVLGVSSL SNDFRDLDEA ASKGNQKAEL
     ALEIFAYKIK KVIGEYIAVL NGVDAIVFTA GIGENSATIR KRILADLDGI GIKIDEEKNK
     IRGQEIDIST PDATVRVLVI PTNEELTIAR DTKEICETEV KLRSSVPI