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UniProtKB/Swiss-Prot entry P27550


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACSA_ECOLI
Primary accession number P27550
Secondary accession number Q2M6N5
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on October 1, 1993 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 72)
Name and origin of the protein
Protein name Acetyl-coenzyme A synthetase
Synonyms EC 6.2.1.1
Acetate--CoA ligase
Acyl-activating enzyme
Gene name
Name: acs
Synonyms: yfaC
OrderedLocusNames: b4069, JW4030
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
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 323-652.
STRAIN=K12;
PubMed=1479344 [NCBI, ExPASy, EBI, Israel, Japan]
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.
PubMed=21941 [NCBI, ExPASy, EBI, Israel, Japan]
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]
CHARACTERIZATION.
PubMed=7751300 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1128/JB.182.15.4173-4179.2000; PubMed=10894724 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1021/bi00156a033; PubMed=1390767 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1046/j.1365-2958.2001.02425.x; PubMed=11359578 [NCBI, ExPASy, EBI, Israel, Japan]
Barak R., Eisenbach M.;
"Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis.";
Mol. Microbiol. 40:731-743(2001).
Comments
  • 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.
  • 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.
  • PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme (By similarity).
  • SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U00006; AAC43163.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77039.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78071.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M87509; AAA24715.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D65215; D65215.
RefSeq AP_004570.1; -.
NP_418493.1; -.
3D structure databases
HSSP Q8ZKF6; 1PG3. [HSSP ENTRY / PDB]
SMR P27550; 5-647.
ModBase P27550.
Enzyme and pathway databases
BioCyc EcoCyc:ACS-MON; -.
MetaCyc:ACS-MON; -.
Organism-specific databases
EchoBASE EB1417; -.
EcoGene EG11448; acs.
Ontologies
GO
GO:0003987; Molecular function: acetate-CoA ligase activity (inferred from electronic annotation from HAMAP).
GO:0016208; Molecular function: AMP binding (inferred from electronic annotation from InterPro).
GO:0008152; Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01123; -; 1.
PBIL [Tree]
InterPro IPR011904; Ac_CoA_lig_AcsA.
IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.
Pfam PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.
PRINTS PR00154; AMPBINDING.
TIGRFAMs TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE PS00455; AMP_BINDING; 1.
BLOCKS P27550.
ProtoNet P27550.
Genome annotation databases
GeneID 948572; -.
GenomeReviews U00096_GR; b4069.
AP009048_GR; JW4030.
KEGG ecj:JW4030; -.
eco:b4069; -.
Phylogenomic databases
HOGENOM P27550; -.
Genome annotation databases
CMR P27550; b4069.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Ligase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   652  652     Acetyl-coenzyme A synthetase. PRO_0000208362
ACT_SITE   517   517        By similarity. 
MOD_RES   609   609        N6-acetyllysine (By similarity). 
Sequence information
Length: 652 AA [This is the length of the unprocessed precursor] Molecular weight: 72094 Da [This is the MW of the unprocessed precursor] CRC64: F464062B6E82C099 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK PYQKVKNTSF 

        70         80         90        100        110        120 
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY KELHRDVCRF 

       130        140        150        160        170        180 
ANTLLELGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS 

       190        200        210        220        230        240 
RLVITSDEGV RAGRSIPLKK NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL 

       250        260        270        280        290        300 
VEQASDQHQA EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ VNILYTAPTA 

       370        380        390        400        410        420 
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGNEKCPVV DTWWQTETGG 

       430        440        450        460        470        480 
FMITPLPGAT ELKAGSATRP FFGVQPALVD NEGNPLEGAT EGSLVITDSW PGQARTLFGD 

       490        500        510        520        530        540 
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP 

       550        560        570        580        590        600 
KIAEAAVVGI PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 

       610        620        630        640        650 
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS 

P27550 in FASTA format

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