ACKA_SALTI
ID ACKA_SALTI Reviewed; 400 AA.
AC P63412; Q8XF99;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020};
GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020};
GN OrderedLocusNames=STY2567, t0527;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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DR EMBL; AL513382; CAD07569.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68233.1; -; Genomic_DNA.
DR RefSeq; NP_456879.1; NC_003198.1.
DR RefSeq; WP_000095689.1; NZ_WSUR01000029.1.
DR AlphaFoldDB; P63412; -.
DR SMR; P63412; -.
DR STRING; 220341.16503561; -.
DR EnsemblBacteria; AAO68233; AAO68233; t0527.
DR KEGG; stt:t0527; -.
DR KEGG; sty:STY2567; -.
DR PATRIC; fig|220341.7.peg.2599; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_0_6; -.
DR OMA; KIITCHI; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
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 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 PANTHER; PTHR21060; PTHR21060; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00016; ackA; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..400
FT /note="Acetate kinase"
FT /id="PRO_0000107608"
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 210..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 285..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 333..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 243
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
SQ SEQUENCE 400 AA; 43257 MW; BD26BC1AB08CA7AD CRC64;
MSSKLVLVLN CGSSSLKFAI IDAVNGDEYL SGLAECFHLP EARIKWKMDG SKQEAALGAG
AAHSEALNFI VNTILAQKPE LSAQLTAIGH RIVHGGEKYT SSVVIDESVI QGIKDSASFA
PLHNPAHLIG IAEALKSFPQ LKDKNVAVFD TAFHQTMPEE SYLYALPYSL YKEHGVRRYG
AHGTSHFYVT QEAAKMLNKP VEELNIITCH LGNGGSVSAI RNGKCVDTSM GLTPLEGLVM
GTRSGDIDPA IIFHLHDTLG MSVDQINKML TKESGLLGLT EVTSDCRYVE DNYATKEDAK
RAMDVYCHRL AKYIGSYTAL MDGRLDAVVF TGGIGENAAM VRELSLGKLG VLGFEVDHER
NLAARFGKSG FINKEGTRPA VVIPTNEELV IAQDASRLTA
