|Gene:||ackA||Accession Numbers: EG10027 (EcoCyc), b2296, ECK2290|
Synonyms: propionate kinase 2, acetate kinase A
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].
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].
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)
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
|Biological Process:||GO:0006083 - acetate metabolic process
GO:0019413 - acetate biosynthetic process [Hesslinger98]
GO:0019542 - propionate biosynthetic process [Hesslinger98]
GO:0042710 - biofilm formation [Wolfe03]
GO:0044011 - single-species biofilm formation on inanimate substrate [Wolfe03]
GO:0006082 - organic acid metabolic process [GOA01a]
GO:0006085 - acetyl-CoA biosynthetic process [UniProtGOA12]
GO:0016310 - phosphorylation [UniProtGOA11a, GOA06, GOA01a]
|Molecular Function:||GO:0008270 - zinc ion binding
GO:0008776 - acetate kinase activity [GOA06, GOA01, Matsuyama89]
GO:0000166 - nucleotide binding [UniProtGOA11a]
GO:0000287 - magnesium ion binding [GOA06]
GO:0005524 - ATP binding [UniProtGOA11a]
GO:0016301 - kinase activity [UniProtGOA11a, GOA01a]
GO:0016740 - transferase activity [UniProtGOA11a]
GO:0016774 - phosphotransferase activity, carboxyl group as acceptor [GOA01a]
GO:0046872 - metal ion binding [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol
[DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane [Lasserre06]
GO:0005622 - intracellular [GOA01a]
GO:0005737 - cytoplasm [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|
|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]
Enzymatic reaction of: acetate kinase
Synonyms: acetokinase, ATP:acetate phosphotransferase
EC Number: 22.214.171.124
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]
Purification of the enzyme was first described from E. coli strain 4157 [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]
pH(opt): 7.4 [ROSE54]
Enzymatic reaction of: propionate kinase (acetate kinase)
EC Number: 126.96.36.199
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.
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].
|Feature Class||Location||Attached Group||Citations||Comment|
|Nucleotide-Phosphate-Binding-Region||210 -> 214||ATP|
|Nucleotide-Phosphate-Binding-Region||285 -> 287||ATP|
|Nucleotide-Phosphate-Binding-Region||333 -> 337||ATP|
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
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
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
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
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
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
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
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
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
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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