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Escherichia coli K-12 substr. MG1655 Enzyme: acetyl-CoA synthetase (AMP-forming)



Gene: acs Accession Numbers: EG11448 (EcoCyc), b4069, ECK4062

Synonyms: yfaC, acsA

Regulation Summary Diagram: ?

Summary:
Acetyl-CoA synthetase (Acs) activates acetate to acetyl-CoA in an ATP-dependent manner [Brown77, Kumari95]. Acs activity constitutes one of two distinct pathways by which E. coli activates acetate to acetyl-CoA. The Acs pathway (acetate conversion to acetyl-CoA) functions in a mainly anabolic role, scavenging acetate present in the extracellular medium. Induction of acs expression functions as the metabolic switch activating this pathway [Kumari00, Valgepea10].

Genetic interactions suggest that Acs is acetylated and thereby inactivated through the action of peptidyl-lysine acetyltransferase, and that CobB catalyzes deacetylation of Acs [CastanoCerezo11].

Acs was thought to be involved in acetylation of CheY [Wolfe88a, Barak92, Barak98, Ramakrishnan98, Barak01, Barak04a]. Acetylation of CheY by Acs in vitro is reversible and cooperative, with a Hill coefcient of 3 [Barak04]. However, acetylation of CheY in vivo is largely a result of autoacetylation [Yan08a]. An acs mutant has a defect in chemotaxis [Barak01], which was not seen by [Li10d].

Based on sequence similarity, Acs has been predicted to be a hydroxycinnamate-CoA ligase [Reed03].

An acs mutant strain grows poorly on solid media with low concentrations of acetate as the sole source of carbon [Kumari95].

Acs activity is induced by growth on acetate [Brown77]. Gene expression is observed during growth on acetate or propionate [Brock02] and at stationary phase [Shin97, Kumari00a]. CsrA positively regulates Acs expression [Wei00]. In a long-term glucose-limited continuous culture experiment, mutants in the acs promoter region that overexpress Acs appeared [Treves98, Kinnersley09].

Citations: [Canovas03, Lin06a, Veit07, Rahman08, CastanoCerezo09, Nahku10, Shin09c, Gonidakis10a, Gonidakis10, Renilla12, MartinezGomez12]

Gene Citations: [Gimenez03]

Locations: cytosol

Map Position: [4,283,436 <- 4,285,394] (92.32 centisomes)
Length: 1959 bp / 652 aa

Molecular Weight of Polypeptide: 72.094 kD (from nucleotide sequence), 72.0 kD (experimental) [Kumari95 ]

Unification Links: ASAP:ABE-0013337 , CGSC:34317 , EchoBASE:EB1417 , EcoGene:EG11448 , EcoliWiki:b4069 , ModBase:P27550 , OU-Microarray:b4069 , PortEco:acs , PR:PRO_000022052 , Pride:P27550 , Protein Model Portal:P27550 , RefSeq:NP_418493 , RegulonDB:EG11448 , SMR:P27550 , String:511145.b4069 , Swiss-Model:P27550 , UniProt:P27550

Relationship Links: InterPro:IN-FAMILY:IPR000873 , InterPro:IN-FAMILY:IPR011904 , InterPro:IN-FAMILY:IPR020845 , InterPro:IN-FAMILY:IPR024597 , InterPro:IN-FAMILY:IPR025110 , Pfam:IN-FAMILY:PF00501 , Pfam:IN-FAMILY:PF11930 , Pfam:IN-FAMILY:PF13193 , Prosite:IN-FAMILY:PS00455

In Paralogous Gene Group: 13 (9 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006476 - protein deacetylation Inferred from experiment [Barak06]
GO:0018394 - peptidyl-lysine acetylation Inferred from experiment [Barak04]
GO:0034421 - post-translational protein acetylation Inferred from experiment [Barak04]
GO:0045733 - acetate catabolic process Inferred from experiment [Kumari95]
GO:0006935 - chemotaxis Inferred by computational analysis [GOA06]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0019427 - acetyl-CoA biosynthetic process from acetate Inferred by computational analysis [GOA06, GOA01]
Molecular Function: GO:0003987 - acetate-CoA ligase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Kumari95]
GO:0033558 - protein deacetylase activity Inferred from experiment [Barak06]
GO:0050218 - propionate-CoA ligase activity Inferred from experiment [Barak04]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0016208 - AMP binding Inferred by computational analysis [GOA01]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism biosynthesis of building blocks fatty acids and phosphatidic acid
metabolism carbon utilization carbon compounds
metabolism carbon utilization fatty acids
metabolism central intermediary metabolism acetate catabolism

Essentiality data for acs knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 03-Aug-2012 by Keseler I , SRI International


Enzymatic reaction of: acetyl-CoA synthetase (AMP-forming)

Synonyms: acetate-CoA ligase, acetyl-coenzyme A synthetase, acyl-activating enzyme, acetyl-activating enzyme, acetate thiokinase, acetate:CoA ligase (AMP-forming)

EC Number: 6.2.1.1

acetate + ATP + coenzyme A <=> acetyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of acetate utilization and formation , acetate conversion to acetyl-CoA

Summary:
Substrate specificity of the enzyme has been determined. Mg2+ can be substituted by Mn2+ and Ca2+ [Barak04].

Cofactors or Prosthetic Groups: Mg2+ [Brown77]

Inhibitors (Competitive): propanoate [Brown77]

Inhibitors (Unknown Mechanism): AMP [Barak04] , diphosphate [Barak04] , EDTA [Brown77]

Primary Physiological Regulators of Enzyme Activity: propanoate

Kinetic Parameters:

Substrate
Km (μM)
Citations
acetate
200.0, 200.0
[Brown77]
ATP
150.0
[Brown77]
coenzyme A
200.0, 200.0
[Brown77]

pH(opt): 8.5 [Brown77]


Enzymatic reaction of: propanoate:CoA ligase (AMP-forming) (acetyl-CoA synthetase (AMP-forming))

EC Number: 6.2.1.17

propanoate + ATP + coenzyme A <=> propanoyl-CoA + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: 2-methylcitrate cycle I

Summary:
The specific activity of Acs towards propionate is 20% of its activity with acetate [Barak04].

Cofactors or Prosthetic Groups: Mg2+


Sequence Features

Feature Class Location Citations Comment
Protein-Segment 191 -> 194
[UniProt13]
UniProt: Coenzyme A; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 311
[UniProt13]
UniProt: Coenzyme A; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 335
[UniProt13]
UniProt: Coenzyme A; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 387
[UniProt13]
UniProt: Substrate; via amide nitrogen; Non-Experimental Qualifier: by similarity.
Protein-Segment 411 -> 416
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 500
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 515
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Active-Site 517
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 523
[UniProt13]
UniProt: Coenzyme A; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 526
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 537
[UniProt13]
UniProt: Magnesium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 539
[UniProt13]
UniProt: Magnesium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 542
[UniProt13]
UniProt: Magnesium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 584
[UniProt13]
UniProt: Coenzyme A; Non-Experimental Qualifier: by similarity.
Acetylation-Modification 609
[Barak04, UniProt13]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b4069 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11448; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Barak01: Barak R, Eisenbach M (2001). "Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis." Mol Microbiol 40(3);731-43. PMID: 11359578

Barak04: Barak R, Prasad K, Shainskaya A, Wolfe AJ, Eisenbach M (2004). "Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli." J Mol Biol 342(2);383-401. PMID: 15327942

Barak04a: Barak R, Eisenbach M (2004). "Co-regulation of acetylation and phosphorylation of CheY, a response regulator in chemotaxis of Escherichia coli." J Mol Biol 342(2);375-81. PMID: 15327941

Barak06: Barak R, Yan J, Shainskaya A, Eisenbach M (2006). "The chemotaxis response regulator CheY can catalyze its own acetylation." J Mol Biol 359(2);251-65. PMID: 16630631

Barak92: Barak R, Welch M, Yanovsky A, Oosawa K, Eisenbach M (1992). "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch." Biochemistry 31(41);10099-107. PMID: 1390767

Barak98: Barak R, Abouhamad WN, Eisenbach M (1998). "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 1998;180(4);985-8. PMID: 9473056

Brock02: Brock M, Maerker C, Schutz A, Volker U, Buckel W (2002). "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase." Eur J Biochem 269(24);6184-94. PMID: 12473114

Brown77: Brown TD, Jones-Mortimer MC, Kornberg HL (1977). "The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli." J Gen Microbiol 1977;102(2);327-36. PMID: 21941

Canovas03: Canovas M, Bernal V, Torroglosa T, Ramirez JL, Iborra JL (2003). "Link between primary and secondary metabolism in the biotransformation of trimethylammonium compounds by escherichia coli." Biotechnol Bioeng 84(6);686-99. PMID: 14595781

CastanoCerezo09: Castano-Cerezo S, Pastor JM, Renilla S, Bernal V, Iborra JL, Canovas M (2009). "An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli." Microb Cell Fact 8;54. PMID: 19852855

CastanoCerezo11: Castano-Cerezo S, Bernal V, Blanco-Catala J, Iborra JL, Canovas M (2011). "cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli." Mol Microbiol 82(5);1110-28. PMID: 22059728

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Gimenez03: Gimenez R, Nunez MF, Badia J, Aguilar J, Baldoma L (2003). "The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli." J Bacteriol 185(21);6448-55. PMID: 14563880

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gonidakis10: Gonidakis S, Finkel SE, Longo VD (2010). "Genome-wide screen identifies Escherichia coli TCA-cycle-related mutants with extended chronological lifespan dependent on acetate metabolism and the hypoxia-inducible transcription factor ArcA." Aging Cell 9(5);868-81. PMID: 20707865

Gonidakis10a: Gonidakis S, Finkel SE, Longo VD (2010). "E. coli hypoxia-inducible factor ArcA mediates lifespan extension in a lipoic acid synthase mutant by suppressing acetyl-CoA synthetase." Biol Chem 391(10);1139-47. PMID: 20707605

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kinnersley09: Kinnersley MA, Holben WE, Rosenzweig F (2009). "E Unibus Plurum: genomic analysis of an experimentally evolved polymorphism in Escherichia coli." PLoS Genet 5(11);e1000713. PMID: 19893610

Kumari00: Kumari S, Beatty CM, Browning DF, Busby SJ, Simel EJ, Hovel-Miner G, Wolfe AJ (2000). "Regulation of acetyl coenzyme A synthetase in Escherichia coli." J Bacteriol 182(15);4173-9. PMID: 10894724

Kumari00a: Kumari S, Simel EJ, Wolfe AJ (2000). "sigma(70) is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli." J Bacteriol 182(2);551-4. PMID: 10629211

Kumari95: Kumari S, Tishel R, Eisenbach M, Wolfe AJ (1995). "Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli." J Bacteriol 1995;177(10);2878-86. PMID: 7751300

Li10d: Li R, Gu J, Chen YY, Xiao CL, Wang LW, Zhang ZP, Bi LJ, Wei HP, Wang XD, Deng JY, Zhang XE (2010). "CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY." Mol Microbiol 76(5):1162-74. PMID: 20345663

Lin06a: Lin H, Castro NM, Bennett GN, San KY (2006). "Acetyl-CoA synthetase overexpression in Escherichia coli demonstrates more efficient acetate assimilation and lower acetate accumulation: a potential tool in metabolic engineering." Appl Microbiol Biotechnol 71(6);870-4. PMID: 16496143

MartinezGomez12: Martinez-Gomez K, Flores N, Castaneda HM, Martinez-Batallar G, Hernandez-Chavez G, Ramirez OT, Gosset G, Encarnacion S, Bolivar F (2012). "New insights into Escherichia coli metabolism: carbon scavenging, acetate metabolism and carbon recycling responses during growth on glycerol." Microb Cell Fact 11;46. PMID: 22513097

Nahku10: Nahku R, Valgepea K, Lahtvee PJ, Erm S, Abner K, Adamberg K, Vilu R (2010). "Specific growth rate dependent transcriptome profiling of Escherichia coli K12 MG1655 in accelerostat cultures." J Biotechnol 145(1);60-5. PMID: 19861135

Rahman08: Rahman M, Hasan MR, Shimizu K (2008). "Growth phase-dependent changes in the expression of global regulatory genes and associated metabolic pathways in Escherichia coli." Biotechnol Lett 30(5);853-60. PMID: 18175070

Ramakrishnan98: Ramakrishnan R, Schuster M, Bourret RB (1998). "Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY." Proc Natl Acad Sci U S A 1998;95(9);4918-23. PMID: 9560203

Reed03: Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)." Genome Biol 4(9);R54. PMID: 12952533

Renilla12: Renilla S, Bernal V, Fuhrer T, Castano-Cerezo S, Pastor JM, Iborra JL, Sauer U, Canovas M (2012). "Acetate scavenging activity in Escherichia coli: interplay of acetyl-CoA synthetase and the PEP-glyoxylate cycle in chemostat cultures." Appl Microbiol Biotechnol 93(5);2109-24. PMID: 21881893

Shin09c: Shin S, Chang DE, Pan JG (2009). "Acetate consumption activity directly determines the level of acetate accumulation during Escherichia coli W3110 growth." J Microbiol Biotechnol 19(10);1127-34. PMID: 19884769

Shin97: Shin S, Song SG, Lee DS, Pan JG, Park C (1997). "Involvement of iclR and rpoS in the induction of acs, the gene for acetyl coenzyme A synthetase of Escherichia coli K-12." FEMS Microbiol Lett 1997;146(1);103-8. PMID: 8997713

Treves98: Treves DS, Manning S, Adams J (1998). "Repeated evolution of an acetate-crossfeeding polymorphism in long-term populations of Escherichia coli." Mol Biol Evol 15(7);789-97. PMID: 9656481

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Valgepea10: Valgepea K, Adamberg K, Nahku R, Lahtvee PJ, Arike L, Vilu R (2010). "Systems biology approach reveals that overflow metabolism of acetate in Escherichia coli is triggered by carbon catabolite repression of acetyl-CoA synthetase." BMC Syst Biol 4(1);166. PMID: 21122111

Veit07: Veit A, Polen T, Wendisch VF (2007). "Global gene expression analysis of glucose overflow metabolism in Escherichia coli and reduction of aerobic acetate formation." Appl Microbiol Biotechnol 74(2);406-21. PMID: 17273855

Wei00: Wei B, Shin S, LaPorte D, Wolfe AJ, Romeo T (2000). "Global regulatory mutations in csrA and rpoS cause severe central carbon stress in Escherichia coli in the presence of acetate." J Bacteriol 182(6);1632-40. PMID: 10692369

Wolfe88a: Wolfe AJ, Conley MP, Berg HC (1988). "Acetyladenylate plays a role in controlling the direction of flagellar rotation." Proc Natl Acad Sci U S A 85(18);6711-5. PMID: 2901103

Yan08a: Yan J, Barak R, Liarzi O, Shainskaya A, Eisenbach M (2008). "In vivo acetylation of CheY, a response regulator in chemotaxis of Escherichia coli." J Mol Biol 376(5);1260-71. PMID: 18234227

Other References Related to Gene Regulation

Beatty03: Beatty CM, Browning DF, Busby SJ, Wolfe AJ (2003). "Cyclic AMP receptor protein-dependent activation of the Escherichia coli acsP2 promoter by a synergistic class III mechanism." J Bacteriol 185(17);5148-57. PMID: 12923087

Browning02: Browning DF, Beatty CM, Wolfe AJ, Cole JA, Busby SJ (2002). "Independent regulation of the divergent Escherichia coli nrfA and acsP1 promoters by a nucleoprotein assembly at a shared regulatory region." Mol Microbiol 43(3);687-701. PMID: 11929525

Browning04a: Browning DF, Beatty CM, Sanstad EA, Gunn KE, Busby SJ, Wolfe AJ (2004). "Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: anti-activation by the nucleoid proteins FIS and IHF." Mol Microbiol 51(1);241-54. PMID: 14651625

Browning05: Browning DF, Grainger DC, Beatty CM, Wolfe AJ, Cole JA, Busby SJ (2005). "Integration of three signals at the Escherichia coli nrf promoter: a role for Fis protein in catabolite repression." Mol Microbiol 57(2);496-510. PMID: 15978080

Browning06: Browning DF, Lee DJ, Wolfe AJ, Cole JA, Busby SJ (2006). "The Escherichia coli K-12 NarL and NarP proteins insulate the nrf promoter from the effects of integration host factor." J Bacteriol 188(21);7449-56. PMID: 16936015

Olvera09: Olvera L, Mendoza-Vargas A, Flores N, Olvera M, Sigala JC, Gosset G, Morett E, Bolivar F (2009). "Transcription analysis of central metabolism genes in Escherichia coli. Possible roles of sigma38 in their expression, as a response to carbon limitation." PLoS One 4(10);e7466. PMID: 19838295

Sclavi07: Sclavi B, Beatty CM, Thach DS, Fredericks CE, Buckle M, Wolfe AJ (2007). "The multiple roles of CRP at the complex acs promoter depend on activation region 2 and IHF." Mol Microbiol 65(2);425-40. PMID: 17630973


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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