ID A0A2H9U5K8_9GAMM Unreviewed; 400 AA.
AC A0A2H9U5K8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CUC53_07885 {ECO:0000313|EMBL:PJG59312.1};
OS Aeromonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1006623 {ECO:0000313|EMBL:PJG59312.1, ECO:0000313|Proteomes:UP000235861};
RN [1] {ECO:0000313|EMBL:PJG59312.1, ECO:0000313|Proteomes:UP000235861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDC 2508 {ECO:0000313|EMBL:PJG59312.1,
RC ECO:0000313|Proteomes:UP000235861};
RA Colston S.M., Navarro A., Martinez-Murcia A.J., Graf J.;
RT "Draft genome sequence of environmental isolate Aeromonas cavernicola sp.
RT nov. MDC 2508.";
RL Submitted (NOV-2017) 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:PJG59312.1}.
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DR EMBL; PGGC01000072; PJG59312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9U5K8; -.
DR OrthoDB; 9802453at2; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000235861; 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:SF19; 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}; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00020}.
FT ACT_SITE 149
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 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 209..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 284..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 332..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 242
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 400 AA; 42898 MW; 915B28D55A282F4E CRC64;
MSKLVLVLNC GSSSLKFAVI DATTGDDLLS GLAECFNLDD ARIKWKLNGE KGSADLGAGA
AHQEALDYIV NKILPLNPEL AANLFAIGHR VVHGGEKFTS SVVITSEVIK GIEDCATLAP
LHNPAHLIGI RAAMKVFPQL ADKNVAVFDT AFHQTMPQEA FLYALPYKLY QENGIRRYGM
HGTSHYYISL EAAKQLNKPV SELNIINCHL GNGGSVCAIK NGQSVDTSMG LTPLEGLVMG
TRCGDIDPAI IFHLHDNLGM SVAEINTMLT KESGLQGLTE VTSDCRFVED NYDSKEEAKR
AMDVYCYRLA KYIGAYAAAM DGRLDAVVFT GGIGENSAPI REMTLNKLAL LGFDVDHAAN
LAARFGKGGE ISKAGSTKAL VIPTNEEWVI AHDALALIGA
//
