ID A0A0M9DQ03_9BACT Unreviewed; 604 AA.
AC A0A0M9DQ03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AD998_00695 {ECO:0000313|EMBL:KOY84860.1};
OS bacterium 336/3.
OC Bacteria.
OX NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY84860.1, ECO:0000313|Proteomes:UP000037950};
RN [1] {ECO:0000313|EMBL:KOY84860.1, ECO:0000313|Proteomes:UP000037950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:KOY84860.1,
RC ECO:0000313|Proteomes:UP000037950};
RA Isojarvi J., Battchikova N., Aro E.-M.;
RT "Draft genome sequence of symbiotic bacteroides-like organism.";
RL Submitted (JUL-2015) 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:KOY84860.1}.
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DR EMBL; LJIE01000001; KOY84860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9DQ03; -.
DR STRING; 1664068.AD998_00695; -.
DR PATRIC; fig|1664068.3.peg.139; -.
DR OrthoDB; 9802453at2; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000037950; 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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 InterPro; IPR008300; PTAC.
DR NCBIfam; TIGR00016; ackA; 1.
DR PANTHER; PTHR21060; ACETATE KINASE; 1.
DR PANTHER; PTHR21060:SF19; ACETATE KINASE; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR Pfam; PF06130; PTAC; 2.
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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000037950};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00020}.
FT ACT_SITE 140
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 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 200..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 274..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 322..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 172
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 233
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 604 AA; 66181 MW; E0092E3BE14716D8 CRC64;
MQILVVNCGS SSVKAEVIDL TSGKRVIVMS VDRISDAQPK LKFSDSEEVL SCPGSGHDQT
LSFAFPLLIK KLDASLLKGV GHRVVHGGKI FDEPVVITED VEKQIDELKS LAPLHNPINL
LGVKIAKKFF PDIPHVAVFD TAFHSTLPPK AKNYALPKSL IDKHHIERYG FHGTSHQYVA
KQAADYLGTD IHDLRIISCH LGNGASVCAI EHGLSVETSM GMTPLEGLVM GTRSGDLDAG
IITYLMEKEG KTWQEISDML NKDSGMKGIA GSNDMRDLEE KAAEGDVNAQ LAIEMFVHRL
RKYIGSYAAV MGGADVLIFT AGIGENSTSL RHKVVQKLNF MRAILDDNKN KMLKFIGVEN
VEEISASNSL CKILVVKTDE QLAIAEQSAK LIKSAKLKDQ GPRSIPIAVS ARHIHLTQES
VDILFGKGYQ LTEHKPLSQP GQFACKEMLT LVGPKNKIEK VRILGPTRPK DQVEISRTDE
FFLGIDAPIR ESGHVEGSPG LTLIGPNGKL DLKEGVICAW RHIHMHPEDA EYFGVKDKDI
VEIRIENQER GLTFGNVLIR VSEKFKLEMH IDTDEANAAE LNQGAEGSLM LTEAGGMLTK
KKIG
//
