ID A0A3M6QA71_9BURK Unreviewed; 400 AA.
AC A0A3M6QA71;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EBQ25_06625 {ECO:0000313|EMBL:RMW99734.1};
OS Allofranklinella schreckenbergeri.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Allofranklinella.
OX NCBI_TaxID=1076744 {ECO:0000313|EMBL:RMW99734.1, ECO:0000313|Proteomes:UP000267035};
RN [1] {ECO:0000313|EMBL:RMW99734.1, ECO:0000313|Proteomes:UP000267035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML161473 {ECO:0000313|EMBL:RMW99734.1,
RC ECO:0000313|Proteomes:UP000267035};
RA Bernier A.-M., Bernard K.;
RT "Comamonadaceae CDC group NO-1 genome sequencing and assembly.";
RL Submitted (OCT-2018) 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:RMW99734.1}.
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DR EMBL; RDQL01000007; RMW99734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M6QA71; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000267035; 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; 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 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:UP000267035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00020}.
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 214..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 289..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 334..338
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 187
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 247
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 400 AA; 42548 MW; A0EFF02FD64B173F CRC64;
MAVNGDWSDC GFLVLNAGSS SLKVALFAAT GDEALLSGKV EKIGPDGVIQ LKDAQGQALP
VAEGVAEGDL GTHTGALMVV IRTIQRHFPA LRLAAVGHRI VHGGPQFNAP LVITPDVMRT
LEALAPFAPL HQPHNLAGVR AAMAAFPGVP QVACFDTAFH RDQPFVNDTF GLPSRYYEQG
VRRYGFHGLS YEYITGQMRQ LAPQLAAGRV VVAHLGNGAS MCAVHDGRAV ASSMGFSPLD
GLAMGTRCGQ IDPGVLLYML DQEKLSSAEI ARVLYHESGL LGLSELSNDM RTLEAAGTPQ
AQRAIDYFVM RAQRELGALA AQLGGLDALV FSGGIGENSV LIRARICERL GWMGIELDPA
RNAEHATWIS AEQARTAVLV VRTHEELVIA RSVRAVVGMA
//
