ACKA_ECOLI
ID ACKA_ECOLI Reviewed; 400 AA.
AC P0A6A3; P15046; P78188; Q59386;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
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}; Synonyms=ack;
GN OrderedLocusNames=b2296, JW2293;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=2536666; DOI=10.1128/jb.171.1.577-580.1989;
RA Matsuyama A., Yamamoto H., Nakano E.;
RT "Cloning, expression, and nucleotide sequence of the Escherichia coli K-12
RT ackA gene.";
RL J. Bacteriol. 171:577-580(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / KH131;
RX PubMed=7883769; DOI=10.1093/oxfordjournals.jbchem.a124616;
RA Kakuda H., Hosono K., Shiroishi K., Ichihara S.;
RT "Identification and characterization of the ackA (acetate kinase A)-pta
RT (phosphotransacetylase) operon and complementation analysis of acetate
RT utilization by an ackA-pta deletion mutant of Escherichia coli.";
RL J. Biochem. 116:916-922(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16080684; DOI=10.1021/bp050073s;
RA Dittrich C.R., Bennett G.N., San K.Y.;
RT "Characterization of the acetate-producing pathways in Escherichia coli.";
RL Biotechnol. Prog. 21:1062-1067(2005).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. During anaerobic growth of
CC the organism, this enzyme is also involved in the synthesis of most of
CC the ATP formed catabolically. The main pathway for acetate production
CC during exponential phase (PubMed:16080684).
CC {ECO:0000269|PubMed:16080684}.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Expressed during exponential phase, decreases as cells enter
CC stationary phase at pH 7.0. Expression is inhibited at pH 6.0. Part of
CC the ackA-pta operon. {ECO:0000269|PubMed:16080684}.
CC -!- DISRUPTION PHENOTYPE: Not essential it can be deleted.
CC {ECO:0000269|PubMed:16080684}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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DR EMBL; M22956; AAA23406.1; -; Genomic_DNA.
DR EMBL; D17576; BAA04501.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75356.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16135.1; -; Genomic_DNA.
DR PIR; JT0498; KIECAA.
DR RefSeq; NP_416799.1; NC_000913.3.
DR RefSeq; WP_000095707.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P0A6A3; -.
DR SMR; P0A6A3; -.
DR BioGRID; 4261690; 455.
DR DIP; DIP-9042N; -.
DR IntAct; P0A6A3; 12.
DR STRING; 511145.b2296; -.
DR SWISS-2DPAGE; P0A6A3; -.
DR jPOST; P0A6A3; -.
DR PaxDb; P0A6A3; -.
DR PRIDE; P0A6A3; -.
DR EnsemblBacteria; AAC75356; AAC75356; b2296.
DR EnsemblBacteria; BAA16135; BAA16135; BAA16135.
DR GeneID; 67416726; -.
DR GeneID; 946775; -.
DR KEGG; ecj:JW2293; -.
DR KEGG; eco:b2296; -.
DR PATRIC; fig|1411691.4.peg.4438; -.
DR EchoBASE; EB0026; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_0_6; -.
DR InParanoid; P0A6A3; -.
DR OMA; KIITCHI; -.
DR PhylomeDB; P0A6A3; -.
DR BioCyc; EcoCyc:ACETATEKINA-MON; -.
DR BioCyc; MetaCyc:ACETATEKINA-MON; -.
DR BRENDA; 2.7.2.1; 2026.
DR SABIO-RK; P0A6A3; -.
DR UniPathway; UPA00340; UER00458.
DR PRO; PR:P0A6A3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008776; F:acetate kinase activity; IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0019413; P:acetate biosynthetic process; IGI:EcoliWiki.
DR GO; GO:0006083; P:acetate metabolic process; IMP:CACAO.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR GO; GO:0019542; P:propionate biosynthetic process; IGI:EcoliWiki.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CACAO.
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 ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="Acetate kinase"
FT /id="PRO_0000107557"
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 CONFLICT 221
FT /note="R -> G (in Ref. 2; BAA04501)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="M -> I (in Ref. 2; BAA04501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 43290 MW; 709C855C514656C8 CRC64;
MSSKLVLVLN CGSSSLKFAI IDAVNGEEYL SGLAECFHLP EARIKWKMDG NKQEAALGAG
AAHSEALNFI VNTILAQKPE LSAQLTAIGH RIVHGGEKYT SSVVIDESVI QGIKDAASFA
PLHNPAHLIG IEEALKSFPQ LKDKNVAVFD TAFHQTMPEE SYLYALPYNL YKEHGIRRYG
AHGTSHFYVT QEAAKMLNKP VEELNIITCH LGNGGSVSAI RNGKCVDTSM GLTPLEGLVM
GTRSGDIDPA IIFHLHDTLG MSVDAINKLL TKESGLLGLT EVTSDCRYVE DNYATKEDAK
RAMDVYCHRL AKYIGAYTAL MDGRLDAVVF TGGIGENAAM VRELSLGKLG VLGFEVDHER
NLAARFGKSG FINKEGTRPA VVIPTNEELV IAQDASRLTA
