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Database: UniProt
Entry: A0A0F5JLZ5_9BACT
LinkDB: A0A0F5JLZ5_9BACT
Original site: A0A0F5JLZ5_9BACT 
ID   A0A0F5JLZ5_9BACT        Unreviewed;       399 AA.
AC   A0A0F5JLZ5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=HMPREF1536_01452 {ECO:0000313|EMBL:KKB58575.1};
OS   Parabacteroides gordonii MS-1 = DSM 23371.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB58575.1, ECO:0000313|Proteomes:UP000033035};
RN   [1] {ECO:0000313|EMBL:KKB58575.1, ECO:0000313|Proteomes:UP000033035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-1 {ECO:0000313|EMBL:KKB58575.1,
RC   ECO:0000313|Proteomes:UP000033035};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA   Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL   Submitted (APR-2013) 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:KKB58575.1}.
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DR   EMBL; AQHW01000009; KKB58575.1; -; Genomic_DNA.
DR   RefSeq; WP_028726350.1; NZ_KQ033919.1.
DR   AlphaFoldDB; A0A0F5JLZ5; -.
DR   STRING; 1203610.HMPREF1536_01452; -.
DR   PATRIC; fig|1203610.3.peg.1487; -.
DR   HOGENOM; CLU_020352_0_1_10; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000033035; 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}; Reference proteome {ECO:0000313|Proteomes:UP000033035};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00020}.
FT   ACT_SITE        148
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         208..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         283..285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         331..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         385
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   SITE            180
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   SITE            241
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   399 AA;  43471 MW;  5B19FD7F899F49EA CRC64;
     MKILVLNCGS SSVKYKLFNM DTHEVLAQGG VEKLGLPGSF LKFTQPDGKK VILDKELPEH
     NAAIEFILSV LTDDKYGCIK SYNEIDAVGH RVVHGGEAFS GSVEITPEVI GKMVECIDLA
     PLHNPPNLKG IRAMSALIPG IRQVGVFDTA FHQTMPDYAY MYGLPYSLYK KYGIRRYGFH
     GTSHRYVSKR ACDILGVPYE EQKIITAHVG NGGSIAAVKN GKSIDTSMGL TPVEGLLMGT
     RCGDVDAGAL TFIMDKEKLD AKGLSDLINK QSGVQGVSGI SSDMREIEAA VADGDKRAIL
     ALNIYNYRIK KYIGAYAAAM GGCDILVWTG GVGENQWATR RVVCENMEYM GMKIDVQKNE
     GMRGEEMVIS TPDSKVTIIV VPTDEEYMIA SDTMDILGK
//
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