|Gene:||pta||Accession Numbers: EG20173 (MetaCyc), b2297, ECK2291|
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of phosphate acetyltransferase / phosphate propionyltransferase = [Pta]6
Phosphate acetyltransferase (Pta) catalyzes the reversible conversion between acetyl-CoA and acetylphosphate, a step in the metabolism of acetate. Both pyruvate and phosphoenolpyruvate activate the enzyme in the direction of acetylphosphate synthesis and inhibit the enzyme in the direction of acetyl-CoA synthesis [CamposBermudez10]. The acetate formation from acetyl-CoA I pathway has been the target of metabolic engineering to reduce the flux to acetate and increase the production of commercially desired end products; see, for example, [Dittrich, De, Shams08, Singh11]. It has also been studied using systems biology approaches such as metabolic modeling and flux balance analysis; see, for example, [Fong06, Young08, Valgepea10].
Pta is composed of three domains; only the C-terminal domain is required for phosphate acetyltransferase activity. The N-terminal domain is involved in stabilization of the native quarternary structure and metabolic regulation [CamposBermudez10].
Pta may be able to utilize both acetyl-CoA and propionyl-CoA. An ack pta double mutant has reduced levels of propionate from L-threonine, suggesting that the enzyme is part of the anaerobic pathway metabolizing L-threonine to propionate [Hesslinger98] (see threonine degradation I).
A pta mutant does not grow on acetate as the sole source of carbon [Brown77]. Both pta and pta ackA mutants are impaired in their ability to survive glucose starvation [Nystrom94]. The growth defect of a pta mutant appears to be due to perturbation of acetyl-CoA flux [Chang99]. pta mutants produce large amounts of lactate when grown on glucose as the carbon source under microaerophilic conditions [Zhu05]. The effect of a pta mutation on metabolism, enzyme activity and gene expression has been thoroughly studied recently [CastanoCerezo09]. pta and recBC mutants are synthetically growth inhibited [Shi05].
Levels of Pta are decreased by growth on acetate [Kirkpatrick01] and under low pH conditions [Stancik02]. pta belongs to the CreBC regulon [Avison01]. FNR has a slightly positive effect on pta expression [ShalelLevanon05]. The growth-rate dependent expression pattern of pta-ackA was measured [Nahku10].
Pta: "phosphotransacetylase" [Brown77]
|Map Position: [2,412,769 -> 2,414,913]|
Molecular Weight of Polypeptide: 77.172 kD (from nucleotide sequence), 81.0 kD (experimental) [YamamotoOtake90 ]
Molecular Weight of Multimer: 484.0 kD (experimental) [CamposBermudez10]
Unification Links: ASAP:ABE-0007582 , CGSC:353 , DIP:DIP-35815N , EchoBASE:EB4147 , EcoGene:EG20173 , EcoliWiki:b2297 , Mint:MINT-1263208 , ModBase:P0A9M8 , OU-Microarray:b2297 , PortEco:pta , PR:PRO_000023627 , Pride:P0A9M8 , Protein Model Portal:P0A9M8 , RefSeq:NP_416800 , RegulonDB:EG20173 , SMR:P0A9M8 , String:511145.b2297 , UniProt:P0A9M8
Relationship Links: InterPro:IN-FAMILY:IPR002505 , InterPro:IN-FAMILY:IPR004614 , InterPro:IN-FAMILY:IPR010766 , InterPro:IN-FAMILY:IPR016475 , InterPro:IN-FAMILY:IPR027417 , Pfam:IN-FAMILY:PF01515 , Pfam:IN-FAMILY:PF07085
|Biological Process:||GO:0006083 - acetate metabolic process
GO:0019413 - acetate biosynthetic process [Brown77]
GO:0019427 - acetyl-CoA biosynthetic process from acetate [Brown77]
GO:0045733 - acetate catabolic process [Brown77]
GO:0070689 - L-threonine catabolic process to propionate [Hesslinger98]
GO:0006085 - acetyl-CoA biosynthetic process [UniProtGOA12]
GO:0008152 - metabolic process [GOA01]
|Molecular Function:||GO:0005515 - protein binding
GO:0008270 - zinc ion binding [Katayama02]
GO:0008959 - phosphate acetyltransferase activity [GOA01a, GOA01, CamposBermudez10, GOLDMAN58]
GO:0016407 - acetyltransferase activity [GOA01]
GO:0016740 - transferase activity [UniProtGOA11]
GO:0016746 - transferase activity, transferring acyl groups [UniProtGOA11, GOA01]
|Cellular Component:||GO:0005829 - cytosol
[DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm [UniProtGOA11a, UniProtGOA11]
|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|
Enzymatic reaction of: phosphate acetyltransferase
Synonyms: phosphotransacetylase, phosphoacylase, acetyl-CoA:orthophosphate acetyltransferase
EC Number: 220.127.116.11
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. [CamposBermudez10]
In Pathways: superpathway of acetate utilization and formation , pyruvate fermentation to acetate IV , superpathway of N-acetylneuraminate degradation , superpathway of lysine degradation , superpathway of taurine degradation , acetate formation from acetyl-CoA I , mixed acid fermentation
The enzyme from E. coli K-12 has only recently been purified and characterized. The enzyme has an eight-fold lower kcat value for the acetylphosphate forming reaction. Km values for CoA and acetyl-CoA are S0.5 values rather than true Km values due to sigmoidal kinetics. Both pyruvate and phosphoenolpyruvate activate the enzyme in the direction of acetylphosphate synthesis and inhibit the enzyme in the direction of acetyl-CoA synthesis. The inhibitory effect of ATP and NADH is reversed in the presence of pyruvate or PEP [CamposBermudez10].
Enzymatic reaction of: phosphate propionyltransferase
EC Number: 18.104.22.168
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.
|Chain||2 -> 714|
|Sequence-Conflict||20 -> 50|
|Sequence-Conflict||208 -> 209|
|Sequence-Conflict||263 -> 271|
|Protein-Segment||391 -> 714|
10/20/97 Gene b2297 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG20173; 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
Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043
CamposBermudez10: Campos-Bermudez VA, Bologna FP, Andreo CS, Drincovich MF (2010). "Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation." FEBS J 277(8);1957-66. PMID: 20236319
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
Chang99: Chang DE, Shin S, Rhee JS, Pan JG (1999). "Acetate metabolism in a pta mutant of Escherichia coli W3110: importance of maintaining acetyl coenzyme A flux for growth and survival." J Bacteriol 181(21);6656-63. PMID: 10542166
De: De Mey M, Lequeux GJ, Beauprez JJ, Maertens J, Van Horen E, Soetaert WK, Vanrolleghem PA, Vandamme EJ "Comparison of different strategies to reduce acetate formation in Escherichia coli." Biotechnol Prog 23(5);1053-63. PMID: 17715942
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
ElMansi06: El-Mansi M, Cozzone AJ, Shiloach J, Eikmanns BJ (2006). "Control of carbon flux through enzymes of central and intermediary metabolism during growth of Escherichia coli on acetate." Curr Opin Microbiol 9(2);173-9. PMID: 16530464
Fong06: Fong SS, Nanchen A, Palsson BO, Sauer U (2006). "Latent pathway activation and increased pathway capacity enable Escherichia coli adaptation to loss of key metabolic enzymes." J Biol Chem 281(12);8024-33. PMID: 16319065
Gupta89: Gupta S, Clark DP (1989). "Escherichia coli derivatives lacking both alcohol dehydrogenase and phosphotransacetylase grow anaerobically by lactate fermentation." J Bacteriol 171(7);3650-5. PMID: 2661531
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
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
Kirkpatrick01: Kirkpatrick C, Maurer LM, Oyelakin NE, Yoncheva YN, Maurer R, Slonczewski JL (2001). "Acetate and formate stress: opposite responses in the proteome of Escherichia coli." J Bacteriol 183(21);6466-77. PMID: 11591692
LeVine80: LeVine SM, Ardeshir F, Ames GF (1980). "Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella typhimurium." J Bacteriol 143(2);1081-5. PMID: 6259116
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
Matsuyama94: Matsuyama A, Yamamoto-Otake H, Hewitt J, MacGillivray RT, Nakano E (1994). "Nucleotide sequence of the phosphotransacetylase gene of Escherichia coli strain K12." Biochim Biophys Acta 1219(2);559-62. PMID: 7918659
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
Nystrom94: Nystrom T (1994). "The glucose-starvation stimulon of Escherichia coli: induced and repressed synthesis of enzymes of central metabolic pathways and role of acetyl phosphate in gene expression and starvation survival." Mol Microbiol 12(5);833-43. PMID: 8052134
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
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
Shi05: Shi IY, Stansbury J, Kuzminov A (2005). "A defect in the acetyl coenzyme A<-->acetate pathway poisons recombinational repair-deficient mutants of Escherichia coli." J Bacteriol 187(4);1266-75. PMID: 15687190
Stancik02: Stancik LM, Stancik DM, Schmidt B, Barnhart DM, Yoncheva YN, Slonczewski JL (2002). "pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli." J Bacteriol 184(15);4246-58. PMID: 12107143
Suzuki69a: Suzuki T, Abiko Y, Shimizu M (1969). "Activation and inhibition of purified phosphotransacetylase of Escherichia coli B by pyruvate and by NADH2 and certain nucleotides." Biochem Biophys Res Commun 35(1);102-8. PMID: 4305270
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;166. PMID: 21122111
Young08: Young JD, Henne KL, Morgan JA, Konopka AE, Ramkrishna D (2008). "Integrating cybernetic modeling with pathway analysis provides a dynamic, systems-level description of metabolic control." Biotechnol Bioeng 100(3);542-59. PMID: 18438875
Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552
Zhu05: Zhu J, Shimizu K (2005). "Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition." Metab Eng 7(2);104-15. PMID: 15781419
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