ACSA_ECOLI
ID ACSA_ECOLI Reviewed; 652 AA.
AC P27550; Q2M6N5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN Name=acs {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=yfaC;
GN OrderedLocusNames=b4069, JW4030;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 299-652.
RC STRAIN=K12;
RX PubMed=1479344; DOI=10.1099/00221287-138-10-2101;
RA Wu G., Williams H.D., Zamanian M., Gibson F., Poole R.K.;
RT "Isolation and characterization of Escherichia coli mutants affected in
RT aerobic respiration: the cloning and nucleotide sequence of ubiG.
RT Identification of an S-adenosylmethionine-binding motif in protein, RNA,
RT and small-molecule methyltransferases.";
RL J. Gen. Microbiol. 138:2101-2112(1992).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=21941; DOI=10.1099/00221287-102-2-327;
RA Brown T.D., Jones-Mortimer M.C., Kornberg H.L.;
RT "The enzymic interconversion of acetate and acetyl-coenzyme A in
RT Escherichia coli.";
RL J. Gen. Microbiol. 102:327-336(1977).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=7751300; DOI=10.1128/jb.177.10.2878-2886.1995;
RA Kumari S., Tishel R., Eisenbach M., Wolfe A.J.;
RT "Cloning, characterization, and functional expression of acs, the gene
RT which encodes acetyl coenzyme A synthetase in Escherichia coli.";
RL J. Bacteriol. 177:2878-2886(1995).
RN [7]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=10894724; DOI=10.1128/jb.182.15.4173-4179.2000;
RA Kumari S., Beatty C.M., Browning D.F., Busby S.J., Simel E.J.,
RA Hovel-Miner G., Wolfe A.J.;
RT "Regulation of acetyl coenzyme A synthetase in Escherichia coli.";
RL J. Bacteriol. 182:4173-4179(2000).
RN [8]
RP ACETYLATION OF CHEY.
RX PubMed=1390767; DOI=10.1021/bi00156a033;
RA Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M.;
RT "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY
RT in vitro and increases its activity at the flagellar switch.";
RL Biochemistry 31:10099-10107(1992).
RN [9]
RP INVOLVEMENT IN CHEMOTAXIS.
RX PubMed=9473056; DOI=10.1128/jb.180.4.985-988.1998;
RA Barak R., Abouhamad W.N., Eisenbach M.;
RT "Both acetate kinase and acetyl coenzyme A synthetase are involved in
RT acetate-stimulated change in the direction of flagellar rotation in
RT Escherichia coli.";
RL J. Bacteriol. 180:985-988(1998).
RN [10]
RP INVOLVEMENT IN CHEMOTAXIS.
RX PubMed=11359578; DOI=10.1046/j.1365-2958.2001.02425.x;
RA Barak R., Eisenbach M.;
RT "Acetylation of the response regulator, CheY, is involved in bacterial
RT chemotaxis.";
RL Mol. Microbiol. 40:731-743(2001).
RN [11]
RP INTERACTION WITH COBB, AND DEACETYLATION.
RX PubMed=15019790; DOI=10.1016/j.jmb.2004.01.060;
RA Zhao K., Chai X., Marmorstein R.;
RT "Structure and substrate binding properties of cobB, a Sir2 homolog protein
RT deacetylase from Escherichia coli.";
RL J. Mol. Biol. 337:731-741(2004).
RN [12]
RP ACETYLATION AT LYS-609.
RX PubMed=15327942; DOI=10.1016/j.jmb.2004.07.020;
RA Barak R., Prasad K., Shainskaya A., Wolfe A.J., Eisenbach M.;
RT "Acetylation of the chemotaxis response regulator CheY by acetyl-CoA
RT synthetase purified from Escherichia coli.";
RL J. Mol. Biol. 342:383-401(2004).
RN [13]
RP DEACETYLATION.
RX PubMed=20345663; DOI=10.1111/j.1365-2958.2010.07125.x;
RA Li R., Gu J., Chen Y.Y., Xiao C.L., Wang L.W., Zhang Z.P., Bi L.J.,
RA Wei H.P., Wang X.D., Deng J.Y., Zhang X.E.;
RT "CobB regulates Escherichia coli chemotaxis by deacetylating the response
RT regulator CheY.";
RL Mol. Microbiol. 76:1162-1174(2010).
CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC an essential intermediate at the junction of anabolic and catabolic
CC pathways. Acs undergoes a two-step reaction. In the first half
CC reaction, Acs combines acetate with ATP to form acetyl-adenylate
CC (AcAMP) intermediate. In the second half reaction, it can then transfer
CC the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC product AcCoA.
CC -!- FUNCTION: Enables the cell to use acetate during aerobic growth to
CC generate energy via the TCA cycle, and biosynthetic compounds via the
CC glyoxylate shunt. Acetylates CheY, the response regulator involved in
CC flagellar movement and chemotaxis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01123, ECO:0000269|PubMed:21941, ECO:0000269|PubMed:7751300};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01123, ECO:0000269|PubMed:21941};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for ATP (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21941};
CC KM=0.2 mM for CoA (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21941};
CC KM=0.2 mM for acetate (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21941};
CC Vmax=100 nmol/min/mg enzyme (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21941};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:21941};
CC -!- SUBUNIT: Forms a 1:1 complex with CobB/NAD-dependent deacetylase.
CC -!- INDUCTION: By CRP and FNR, in response to rising cAMP levels, falling
CC oxygen partial pressure and changes in carbon flux. May also be induced
CC by acetate. {ECO:0000269|PubMed:10894724}.
CC -!- PTM: Autoacetylated. Deacetylation by CobB activates the enzyme.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow as well as wild-type
CC cells at high concentrations (>25 mM) of acetate as the sole carbon
CC source, but grow poorly on lower concentrations (<10 mM).
CC {ECO:0000269|PubMed:7751300}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01123}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24715.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00006; AAC43163.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77039.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78071.1; -; Genomic_DNA.
DR EMBL; M87509; AAA24715.1; ALT_FRAME; Genomic_DNA.
DR PIR; D65215; D65215.
DR RefSeq; NP_418493.1; NC_000913.3.
DR RefSeq; WP_000078239.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P27550; -.
DR SMR; P27550; -.
DR BioGRID; 4262675; 22.
DR IntAct; P27550; 8.
DR STRING; 511145.b4069; -.
DR iPTMnet; P27550; -.
DR jPOST; P27550; -.
DR PaxDb; P27550; -.
DR PRIDE; P27550; -.
DR EnsemblBacteria; AAC77039; AAC77039; b4069.
DR EnsemblBacteria; BAE78071; BAE78071; BAE78071.
DR GeneID; 66672015; -.
DR GeneID; 948572; -.
DR KEGG; ecj:JW4030; -.
DR KEGG; eco:b4069; -.
DR PATRIC; fig|1411691.4.peg.2635; -.
DR EchoBASE; EB1417; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_6; -.
DR InParanoid; P27550; -.
DR OMA; DHWWHDL; -.
DR PhylomeDB; P27550; -.
DR BioCyc; EcoCyc:ACS-MON; -.
DR BioCyc; MetaCyc:ACS-MON; -.
DR SABIO-RK; P27550; -.
DR PRO; PR:P27550; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:CACAO.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IDA:EcoCyc.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:CACAO.
DR GO; GO:0045733; P:acetate catabolic process; IMP:EcoCyc.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:CACAO.
DR GO; GO:0034421; P:post-translational protein acetylation; IDA:CACAO.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR HAMAP; MF_01123; Ac_CoA_synth; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..652
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208362"
FT BINDING 191..194
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 311
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 335
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 387..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 411..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 523
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 584
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT MOD_RES 609
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123,
FT ECO:0000269|PubMed:1390767"
SQ SEQUENCE 652 AA; 72094 MW; F464062B6E82C099 CRC64;
MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK PYQKVKNTSF
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF
ANTLLELGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS
RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL
VEQASDQHQA EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ VNILYTAPTA
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGNEKCPVV DTWWQTETGG
FMITPLPGAT ELKAGSATRP FFGVQPALVD NEGNPLEGAT EGSLVITDSW PGQARTLFGD
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP
KIAEAAVVGI PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS
