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Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme)

 ACSA_ECOLI              Reviewed;         652 AA.
P27550; Q2M6N5;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
Name=acs {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=yfaC;
OrderedLocusNames=b4069, JW4030;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8265357; DOI=10.1093/nar/21.23.5408;
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the
region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 299-652.
STRAIN=K12;
PubMed=1479344; DOI=10.1099/00221287-138-10-2101;
Wu G., Williams H.D., Zamanian M., Gibson F., Poole R.K.;
"Isolation and characterization of Escherichia coli mutants affected
in aerobic respiration: the cloning and nucleotide sequence of ubiG.
Identification of an S-adenosylmethionine-binding motif in protein,
RNA, and small-molecule methyltransferases.";
J. Gen. Microbiol. 138:2101-2112(1992).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
COFACTOR.
PubMed=21941; DOI=10.1099/00221287-102-2-327;
Brown T.D., Jones-Mortimer M.C., Kornberg H.L.;
"The enzymic interconversion of acetate and acetyl-coenzyme A in
Escherichia coli.";
J. Gen. Microbiol. 102:327-336(1977).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=7751300; DOI=10.1128/jb.177.10.2878-2886.1995;
Kumari S., Tishel R., Eisenbach M., Wolfe A.J.;
"Cloning, characterization, and functional expression of acs, the gene
which encodes acetyl coenzyme A synthetase in Escherichia coli.";
J. Bacteriol. 177:2878-2886(1995).
[7]
INDUCTION.
STRAIN=K12;
PubMed=10894724; DOI=10.1128/JB.182.15.4173-4179.2000;
Kumari S., Beatty C.M., Browning D.F., Busby S.J., Simel E.J.,
Hovel-Miner G., Wolfe A.J.;
"Regulation of acetyl coenzyme A synthetase in Escherichia coli.";
J. Bacteriol. 182:4173-4179(2000).
[8]
ACETYLATION OF CHEY.
PubMed=1390767; DOI=10.1021/bi00156a033;
Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M.;
"Acetyladenylate or its derivative acetylates the chemotaxis protein
CheY in vitro and increases its activity at the flagellar switch.";
Biochemistry 31:10099-10107(1992).
[9]
INVOLVEMENT IN CHEMOTAXIS.
PubMed=9473056;
Barak R., Abouhamad W.N., Eisenbach M.;
"Both acetate kinase and acetyl coenzyme A synthetase are involved in
acetate-stimulated change in the direction of flagellar rotation in
Escherichia coli.";
J. Bacteriol. 180:985-988(1998).
[10]
INVOLVEMENT IN CHEMOTAXIS.
PubMed=11359578; DOI=10.1046/j.1365-2958.2001.02425.x;
Barak R., Eisenbach M.;
"Acetylation of the response regulator, CheY, is involved in bacterial
chemotaxis.";
Mol. Microbiol. 40:731-743(2001).
[11]
INTERACTION WITH COBB, AND DEACETYLATION.
PubMed=15019790; DOI=10.1016/j.jmb.2004.01.060;
Zhao K., Chai X., Marmorstein R.;
"Structure and substrate binding properties of cobB, a Sir2 homolog
protein deacetylase from Escherichia coli.";
J. Mol. Biol. 337:731-741(2004).
[12]
AUTOACETYLATION AT LYS-609.
PubMed=15327942; DOI=10.1016/j.jmb.2004.07.020;
Barak R., Prasad K., Shainskaya A., Wolfe A.J., Eisenbach M.;
"Acetylation of the chemotaxis response regulator CheY by acetyl-CoA
synthetase purified from Escherichia coli.";
J. Mol. Biol. 342:383-401(2004).
[13]
DEACETYLATION.
PubMed=20345663; DOI=10.1111/j.1365-2958.2010.07125.x;
Li R., Gu J., Chen Y.Y., Xiao C.L., Wang L.W., Zhang Z.P., Bi L.J.,
Wei H.P., Wang X.D., Deng J.Y., Zhang X.E.;
"CobB regulates Escherichia coli chemotaxis by deacetylating the
response regulator CheY.";
Mol. Microbiol. 76:1162-1174(2010).
-!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
(AcCoA), an essential intermediate at the junction of anabolic and
catabolic pathways. Acs undergoes a two-step reaction. In the
first half reaction, Acs combines acetate with ATP to form acetyl-
adenylate (AcAMP) intermediate. In the second half reaction, it
can then transfer the acetyl group from AcAMP to the sulfhydryl
group of CoA, forming the product AcCoA.
-!- FUNCTION: Enables the cell to use acetate during aerobic growth to
generate energy via the TCA cycle, and biosynthetic compounds via
the glyoxylate shunt. Acetylates CheY, the response regulator
involved in flagellar movement and chemotaxis.
-!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21941, ECO:0000269|PubMed:7751300}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21941};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.15 mM for ATP (at pH 8.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:21941};
KM=0.2 mM for CoA (at pH 8.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:21941};
KM=0.2 mM for acetate (at pH 8.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:21941};
Vmax=100 nmol/min/mg enzyme (at pH 8.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:21941};
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:21941};
-!- SUBUNIT: Forms a 1:1 complex with CobB/NAD-dependent deacetylase.
-!- INDUCTION: By CRP and FNR, in response to rising cAMP levels,
falling oxygen partial pressure and changes in carbon flux. May
also be induced by acetate. {ECO:0000269|PubMed:10894724}.
-!- PTM: Autoacetylated. Deacetylation by CobB activates the enzyme.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene grow as well as
wild-type cells at high concentrations (>25 mM) of acetate as the
sole carbon source, but grow poorly on lower concentrations (<10
mM). {ECO:0000269|PubMed:7751300}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000255|HAMAP-Rule:MF_01123}.
-!- SEQUENCE CAUTION:
Sequence=AAA24715.1; Type=Frameshift; Positions=323; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U00006; AAC43163.1; -; Genomic_DNA.
EMBL; U00096; AAC77039.1; -; Genomic_DNA.
EMBL; AP009048; BAE78071.1; -; Genomic_DNA.
EMBL; M87509; AAA24715.1; ALT_FRAME; Genomic_DNA.
PIR; D65215; D65215.
RefSeq; NP_418493.1; NC_000913.3.
RefSeq; WP_000078239.1; NZ_LN832404.1.
ProteinModelPortal; P27550; -.
SMR; P27550; -.
BioGrid; 4262675; 10.
IntAct; P27550; 7.
STRING; 316385.ECDH10B_4259; -.
iPTMnet; P27550; -.
PaxDb; P27550; -.
PRIDE; P27550; -.
EnsemblBacteria; AAC77039; AAC77039; b4069.
EnsemblBacteria; BAE78071; BAE78071; BAE78071.
GeneID; 948572; -.
KEGG; ecj:JW4030; -.
KEGG; eco:b4069; -.
PATRIC; fig|1411691.4.peg.2635; -.
EchoBASE; EB1417; -.
EcoGene; EG11448; acs.
eggNOG; ENOG4108IQF; Bacteria.
eggNOG; COG0365; LUCA.
HOGENOM; HOG000229981; -.
InParanoid; P27550; -.
KO; K01895; -.
PhylomeDB; P27550; -.
BioCyc; EcoCyc:ACS-MONOMER; -.
BioCyc; MetaCyc:ACS-MONOMER; -.
SABIO-RK; P27550; -.
PRO; PR:P27550; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0003987; F:acetate-CoA ligase activity; IDA:CACAO.
GO; GO:0016208; F:AMP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050218; F:propionate-CoA ligase activity; IDA:EcoCyc.
GO; GO:0033558; F:protein deacetylase activity; IDA:CACAO.
GO; GO:0045733; P:acetate catabolic process; IMP:EcoCyc.
GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:CACAO.
GO; GO:0034421; P:post-translational protein acetylation; IDA:CACAO.
CDD; cd05966; ACS; 1.
HAMAP; MF_01123; Ac_CoA_synth; 1.
InterPro; IPR011904; Ac_CoA_lig.
InterPro; IPR032387; ACAS_N.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF16177; ACAS_N; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium;
Metal-binding; Nucleotide-binding; Reference proteome.
CHAIN 1 652 Acetyl-coenzyme A synthetase.
/FTId=PRO_0000208362.
NP_BIND 387 389 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
NP_BIND 411 416 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
REGION 191 194 Coenzyme A binding. {ECO:0000255|HAMAP-
Rule:MF_01123}.
METAL 537 537 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
METAL 539 539 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
METAL 542 542 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 311 311 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123}.
BINDING 335 335 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123}.
BINDING 500 500 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 515 515 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 523 523 Coenzyme A; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 526 526 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 584 584 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123}.
MOD_RES 609 609 N6-acetyllysine. {ECO:0000255|HAMAP-
Rule:MF_01123,
ECO:0000269|PubMed:1390767}.
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


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