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Database: UniProt
Entry: A0A1Q3WMT4_9BACT
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ID   A0A1Q3WMT4_9BACT        Unreviewed;       388 AA.
AC   A0A1Q3WMT4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BGO59_03150 {ECO:0000313|EMBL:OJW76138.1};
OS   Spirosoma sp. 48-14.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW76138.1, ECO:0000313|Proteomes:UP000186057};
RN   [1] {ECO:0000313|EMBL:OJW76138.1, ECO:0000313|Proteomes:UP000186057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=48-14 {ECO:0000313|EMBL:OJW76138.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00020}.
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:OJW76138.1}.
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DR   EMBL; MKUD01000027; OJW76138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3WMT4; -.
DR   STRING; 1895854.BGO59_03150; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000186057; 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   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; 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};
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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00020}.
FT   ACT_SITE        142
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         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         201..205
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         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   SITE            173
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   SITE            234
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   388 AA;  42010 MW;  14F6C15BB4D88B06 CRC64;
     MSSQLLVLNS GSSSIKFAVY DLAERRIASG KLTRIGQATG AFERTDGHQT NTDALALPDH
     TAALNVLFDW LHQQSHLYIG AIGHRMVHGG ERYWTPQRVT DGLLADLRLL IPLAPDHLPA
     EISLIEAVAA QYPQLPQVVC FDTAFHHSMP ALARRLPVPR YLAEEGVIRY GFHGLSYEYV
     MTRLRQDAGD DVANGRVVLA HLGNGASMAA VRQGKCMDTT MGFTPTGGLM MGTRTGDLDP
     GVVLYLLNHR GLESSELSRL LNDESGLLGV SGTSSDMQTL LQLEPDPPAA AEAIALFCYL
     AAKQLGALVT VLNGLDTLVF TGGIGENAPT IRARICERLA YLGIMLDPTR NQASQAVISP
     EGHLPVVRVI PADEEVMIAR YTRQVLQV
//
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