ACKA_SALTY
ID ACKA_SALTY Reviewed; 400 AA.
AC P63411; Q8XF99;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Acetate kinase AckA {ECO:0000305};
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}; OrderedLocusNames=STM2337;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=26448059; DOI=10.1111/mmi.13243;
RA Moore T.C., Escalante-Semerena J.C.;
RT "The EutQ and EutP proteins are novel acetate kinases involved in
RT ethanolamine catabolism: physiological implications for the function of the
RT ethanolamine metabolosome in Salmonella enterica.";
RL Mol. Microbiol. 99:497-511(2016).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CITRATE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, COFACTOR, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=23031654; DOI=10.1186/1472-6807-12-24;
RA Chittori S., Savithri H.S., Murthy M.R.;
RT "Structural and mechanistic investigations on Salmonella typhimurium
RT acetate kinase (AckA): identification of a putative ligand binding pocket
RT at the dimeric interface.";
RL BMC Struct. Biol. 12:24-24(2012).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. Has broad substrate
CC specificity and can also utilize GTP, UTP and CTP. Can also
CC phosphorylate propionate, but has very low activity with formate and is
CC inactive with butyrate. {ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:23031654}.
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, ECO:0000269|PubMed:23031654};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:23031654};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:23031654};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:23031654};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, butyrate and citrate.
CC {ECO:0000269|PubMed:23031654}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for ATP {ECO:0000269|PubMed:23031654};
CC KM=0.1 mM for ADP {ECO:0000269|PubMed:23031654};
CC KM=1.2 mM for acetate {ECO:0000269|PubMed:23031654};
CC KM=11.2 mM for propionate {ECO:0000269|PubMed:23031654};
CC KM=0.28 mM for acetyl phosphate {ECO:0000269|PubMed:23031654};
CC Vmax=1550 umol/min/mg enzyme with acetate
CC {ECO:0000269|PubMed:23031654};
CC pH dependence:
CC Optimum pH is 7.2-7.5. {ECO:0000269|PubMed:23031654};
CC Temperature dependence:
CC Optimum temperature is 35-37 degrees Celsius.
CC {ECO:0000269|PubMed:23031654};
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 ECO:0000269|PubMed:23031654}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- DISRUPTION PHENOTYPE: Does not grow on ethanolamine and tetrathionate
CC under anoxic conditions; complemented by acetate kinases EutQ.
CC {ECO:0000269|PubMed:26448059}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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DR EMBL; AE006468; AAL21238.1; -; Genomic_DNA.
DR RefSeq; NP_461279.1; NC_003197.2.
DR RefSeq; WP_000095689.1; NC_003197.2.
DR PDB; 3SK3; X-ray; 1.90 A; A/B=1-400.
DR PDB; 3SLC; X-ray; 2.70 A; A/B/C/D=1-400.
DR PDBsum; 3SK3; -.
DR PDBsum; 3SLC; -.
DR AlphaFoldDB; P63411; -.
DR SMR; P63411; -.
DR STRING; 99287.STM2337; -.
DR PaxDb; P63411; -.
DR EnsemblBacteria; AAL21238; AAL21238; STM2337.
DR GeneID; 1253859; -.
DR KEGG; stm:STM2337; -.
DR PATRIC; fig|99287.12.peg.2474; -.
DR HOGENOM; CLU_020352_0_0_6; -.
DR OMA; KIITCHI; -.
DR PhylomeDB; P63411; -.
DR BioCyc; SENT99287:STM2337-MON; -.
DR BRENDA; 2.7.2.1; 5542.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008776; F:acetate kinase activity; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047900; F:formate kinase activity; IDA:CACAO.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008980; F:propionate kinase activity; IDA:CACAO.
DR GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="Acetate kinase AckA"
FT /id="PRO_0000107607"
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"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3SK3"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:3SK3"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3SK3"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3SK3"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3SLC"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:3SLC"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3SK3"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3SLC"
FT HELIX 296..316
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:3SK3"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3SK3"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:3SK3"
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
