Escherichia coli K-12 substr. MG1655 Enzyme: acetate kinase

Gene: ackA Accession Numbers: EG10027 (EcoCyc), b2296, ECK2290

Synonyms: propionate kinase 2, acetate kinase A

Regulation Summary Diagram: ?

Regulation summary diagram for ackA

AckA has propionate kinase activity as well as acetate kinase activity. The ackA-encoded propionate kinase 2 has an important role in propionyl-CoA metabolism [Hesslinger98]. Acetate kinase can also catalyze acetylation of CheY, increasing signal strength for flagellar rotation [Ramakrishnan98, Barak98].

A second gene encoding acetate kinase, ackB, was thought to exist [Pascal81].

Transcription of ackA is induced by the CreBC two-component system by minimal media growth conditions [Avison01].

E. coli double mutants deficient in AckA and Pta activity, or AckA and TdcD activity, were unable to metabolize threonine to propionate. This suggested the participation of this enzyme in pathway L-threonine degradation I. An ackA mutant showed a significant reduction in the conversion of threonine to propionate, as well as a 75% reduction in acetate production [Hesslinger98].

In E. coli acetylphosphate formation via the products of pta and ackA (as in pathway acetate formation from acetyl-CoA I) is the only source of this key metabolite. Acetylphosphate is involved in many cellular processes including the protein quality control system [Mizrahi06, Mizrahi09] and it acts as a global signal regulator [Klein07].

An ackA-negative mutant was unable to utilize xylose in minimal medium under anaerobic conditions. This suggested that ATP generated from the conversion of acetylphosphate to acetate is necessary for growth under these conditions [Hasona04]. In other metabolic engineering studies, pta and ackA negative mutants were used to conserve acetyl-CoA for succinate production in E. coli [Sanchez05a]. Differences in acetate production among E. coli strains have been described [Phue10].

Reviews: [Wolfe05, De07a]

Gene Citations: [Matsuyama89, Kakuda94, Pruss94a]

Locations: cytosol, membrane

Map Position: [2,411,492 -> 2,412,694] (51.98 centisomes, 187°)
Length: 1203 bp / 400 aa

Molecular Weight of Polypeptide: 43.29 kD (from nucleotide sequence)

Isozyme Sequence Similarity [Comment 1]:
propionate kinase: YES

Unification Links: ASAP:ABE-0007579 , CGSC:1048 , DIP:DIP-9042N , EchoBASE:EB0026 , EcoGene:EG10027 , EcoliWiki:b2296 , ModBase:P0A6A3 , OU-Microarray:b2296 , PortEco:ackA , PR:PRO_000022041 , Pride:P0A6A3 , Protein Model Portal:P0A6A3 , RefSeq:NP_416799 , RegulonDB:EG10027 , SMR:P0A6A3 , String:511145.b2296 , UniProt:P0A6A3

Relationship Links: InterPro:IN-FAMILY:IPR000890 , InterPro:IN-FAMILY:IPR004372 , InterPro:IN-FAMILY:IPR023865 , Panther:IN-FAMILY:PTHR21060 , PDB:Structure:1LRG , Pfam:IN-FAMILY:PF00871 , Prints:IN-FAMILY:PR00471 , Prosite:IN-FAMILY:PS01075 , Prosite:IN-FAMILY:PS01076

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for ackA

GO Terms:

Biological Process: GO:0006083 - acetate metabolic process Inferred from experiment [Brown77a]
GO:0019413 - acetate biosynthetic process Inferred from experiment [Hesslinger98]
GO:0019542 - propionate biosynthetic process Inferred from experiment [Hesslinger98]
GO:0042710 - biofilm formation Inferred from experiment [Wolfe03]
GO:0044011 - single-species biofilm formation on inanimate substrate Inferred from experiment [Wolfe03]
GO:0006082 - organic acid metabolic process Inferred by computational analysis [GOA01a]
GO:0006085 - acetyl-CoA biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
Molecular Function: GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0008776 - acetate kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Matsuyama89]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016774 - phosphotransferase activity, carboxyl group as acceptor Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism carbon utilization amino acids
metabolism carbon utilization carbon compounds
metabolism central intermediary metabolism acetate catabolism
metabolism central intermediary metabolism pyruvate oxidation
metabolism central intermediary metabolism threonine catabolism

Essentiality data for ackA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
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]

Last-Curated ? 14-Nov-2011 by Fulcher C , SRI International

Enzymatic reaction of: acetate kinase

Synonyms: acetokinase, ATP:acetate phosphotransferase

EC Number:

acetate + ATP <=> acetyl phosphate + ADP

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

This reaction is reversible. [ROSE54]

In Pathways: superpathway of acetate utilization and formation , acetate formation from acetyl-CoA I , mixed acid fermentation

Purification of the enzyme was first described from E. coli strain 4157 [ROSE54].

Cofactors or Prosthetic Groups: Mg2+ [ROSE54]

Cofactor Binding Comment: A phosphoenzyme intermediate is formed during the reaction and requires enzyme-bound MgADP for phosphorylation of the enzyme by acetylphosphate. [Skarstedt76]

Inhibitors (Unknown Mechanism): p-chloromercuribenzoate [ROSE54]

pH(opt): 7.4 [ROSE54]

Enzymatic reaction of: propionate kinase (acetate kinase)

EC Number:

ATP + propanoate <=> ADP + propanoyl phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: superpathway of L-threonine metabolism , L-threonine degradation I

Purification of the enzyme was first described from E. coli strain 4157. The reaction rate with propionate was approximately 10% of that with acetate [ROSE54].

Sequence Features

Protein sequence of acetate kinase with features indicated

Feature Class Location Attached Group Citations Comment
Metal-Binding-Site 10  
UniProt: Magnesium; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 17  
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 91  
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Active-Site 150  
UniProt: Proton donor/acceptor; Non-Experimental Qualifier: by similarity.
Amino-Acid-Site 182  
UniProt: Transition state stabilizer; Sequence Annotation Type: site; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 210 -> 214 ATP
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Sequence-Conflict 221  
[Kakuda94, UniProt10]
UniProt: (in Ref. 2; BAA04501);
Sequence-Conflict 240  
[Kakuda94, UniProt10]
UniProt: (in Ref. 2; BAA04501);
Amino-Acid-Site 243  
UniProt: Transition state stabilizer; Sequence Annotation Type: site; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 285 -> 287 ATP
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 333 -> 337 ATP
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 387  
UniProt: Magnesium; Non-Experimental Qualifier: by similarity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b2296 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10027; confirmed by SwissProt match.


Avison01: Avison MB, Horton RE, Walsh TR, Bennett PM (2001). "Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media." J Biol Chem 276(29);26955-61. PMID: 11350954

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

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

Brown77a: 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

De07a: De Mey M, De Maeseneire S, Soetaert W, Vandamme E (2007). "Minimizing acetate formation in E. coli fermentations." J Ind Microbiol Biotechnol 34(11);689-700. PMID: 17668256

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

Hasona04: Hasona A, Kim Y, Healy FG, Ingram LO, Shanmugam KT (2004). "Pyruvate formate lyase and acetate kinase are essential for anaerobic growth of Escherichia coli on xylose." J Bacteriol 186(22);7593-600. PMID: 15516572

Hesslinger98: Hesslinger C, Fairhurst SA, Sawers G (1998). "Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate." Mol Microbiol 1998;27(2);477-92. PMID: 9484901

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

Kakuda94: Kakuda H, Hosono K, Shiroishi K, Ichihara S (1994). "Identification and characterization of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli." J Biochem 116(4);916-22. PMID: 7883769

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Klein07: Klein AH, Shulla A, Reimann SA, Keating DH, Wolfe AJ (2007). "The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators." J Bacteriol 189(15);5574-81. PMID: 17545286

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Matsuyama89: Matsuyama A, Yamamoto H, Nakano E (1989). "Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene." J Bacteriol 1989;171(1);577-80. PMID: 2536666

Mizrahi06: Mizrahi I, Biran D, Ron EZ (2006). "Requirement for the acetyl phosphate pathway in Escherichia coli ATP-dependent proteolysis." Mol Microbiol 62(1);201-11. PMID: 16987178

Mizrahi09: Mizrahi I, Biran D, Ron EZ (2009). "Involvement of the Pta-AckA pathway in protein folding and aggregation." Res Microbiol 160(1);80-4. PMID: 19026742

Pascal81: Pascal MC, Chippaux M, Abou-Jaoude A, Blaschkowski HP, Knappe J (1981). "Mutants of Escherichia coli K12 with defects in anaerobic pyruvate metabolism." J Gen Microbiol 1981;124(Pt 1);35-42. PMID: 7033467

Phue10: Phue JN, Lee SJ, Kaufman JB, Negrete A, Shiloach J (2010). "Acetate accumulation through alternative metabolic pathways in ackA (-) pta (-) poxB (-) triple mutant in E. coli B (BL21)." Biotechnol Lett 32(12);1897-903. PMID: 20703804

Pruss94a: Pruss BM, Wolfe AJ (1994). "Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli." Mol Microbiol 1994;12(6);973-84. PMID: 7934904

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

ROSE54: Rose IA, Grunberg-Manago M, Korey SR, Ochoa S (1954). "Enzymatic phosphorylation of acetate." J Biol Chem 211(2);737-56. PMID: 13221579

Sanchez05a: Sanchez AM, Bennett GN, San KY (2005). "Novel pathway engineering design of the anaerobic central metabolic pathway in Escherichia coli to increase succinate yield and productivity." Metab Eng 7(3);229-39. PMID: 15885621

Skarstedt76: Skarstedt MT, Silverstein E (1976). "Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics." J Biol Chem 1976;251(21);6775-83. PMID: 185218

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

UniProt14: UniProt Consortium (2014). "UniProt version 2014-01 released on 2014-01-01 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Wolfe03: Wolfe AJ, Chang DE, Walker JD, Seitz-Partridge JE, Vidaurri MD, Lange CF, Pruss BM, Henk MC, Larkin JC, Conway T (2003). "Evidence that acetyl phosphate functions as a global signal during biofilm development." Mol Microbiol 48(4);977-88. PMID: 12753190

Wolfe05: Wolfe AJ (2005). "The acetate switch." Microbiol Mol Biol Rev 69(1);12-50. PMID: 15755952

Other References Related to Gene Regulation

GamaCastro08: Gama-Castro S, Jimenez-Jacinto V, Peralta-Gil M, Santos-Zavaleta A, Penaloza-Spinola MI, Contreras-Moreira B, Segura-Salazar J, Muniz-Rascado L, Martinez-Flores I, Salgado H, Bonavides-Martinez C, Abreu-Goodger C, Rodriguez-Penagos C, Miranda-Rios J, Morett E, Merino E, Huerta AM, Trevino-Quintanilla L, Collado-Vides J (2008). "RegulonDB (version 6.0): gene regulation model of Escherichia coli K-12 beyond transcription, active (experimental) annotated promoters and Textpresso navigation." Nucleic Acids Res 36(Database issue);D120-4. PMID: 18158297

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

ShalelLevanon05: Shalel-Levanon S, San KY, Bennett GN (2005). "Effect of ArcA and FNR on the expression of genes related to the oxygen regulation and the glycolysis pathway in Escherichia coli under microaerobic growth conditions." Biotechnol Bioeng 92(2):147-59. PMID: 15988767

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Oct 9, 2015, biocyc12.