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Escherichia coli K-12 substr. MG1655 Enzyme: acetoacetyl-CoA transferase

Subunit composition of acetoacetyl-CoA transferase = [(AtoA)2][(AtoD)2]
         β complex = (AtoA)2
                 acetyl-CoA:acetoacetyl-CoA transferase, β subunit = AtoA
         α complex = (AtoD)2
                 acetyl-CoA:acetoacetyl-CoA transferase, α subunit = AtoD

Summary:
The growth of E. coli on short-chain fatty acids (C3-C6) requires the activation of the acids to their respective thioesters. This activation is catalyzed by acetoacetyl-CoA transferase [Sramek75]. The reaction takes place in two half-reactions which involves a covalent enzyme-CoA [Sramek75a]. The enzyme undergoes two detectable conformational changes during the reaction [Sramek77]. It is thought likely that the reaction proceeds by a ping-pong mechanism [Sramek75a]. The enzyme can utilize a variety of short-chain acyl-CoA and carboxylic acid substrates but exhibits maximal activity with normal and 3-keto substrates [Sramek75].

Molecular Weight: 97 kD (experimental) [Sramek75 ]

Gene-Reaction Schematic: ?


Enzymatic reaction of: acetoacetyl-CoA transferase

Synonyms: acetyl-CoA:acetoacetate-CoA transferase

EC Number: 2.8.3.-

acetoacetate + acetyl-CoA <=> acetoacetyl-CoA + acetate

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.

Alternative Substrates [Comment 1]:

In Pathways: acetoacetate degradation (to acetyl CoA)

Citations: [Sramek75a]

Inhibitors (Competitive): acetyl-CoA , coenzyme A [Comment 2]

Inhibitors (Unknown Mechanism): p-chloromercuribenzoate [Sramek75]


Subunit of acetoacetyl-CoA transferase: β complex

Gene: atoA Accession Numbers: EG11670 (EcoCyc), b2222, ECK2215

Locations: cytosol

Subunit composition of β complex = [AtoA]2
         acetyl-CoA:acetoacetyl-CoA transferase, β subunit = AtoA

Map Position: [2,322,131 -> 2,322,781] (50.05 centisomes)
Length: 651 bp / 216 aa

Molecular Weight of Polypeptide: 22.96 kD (from nucleotide sequence), 26 kD (experimental) [Jenkins87a ]

GO Terms:

Biological Process: GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0019395 - fatty acid oxidation
GO:0046459 - short-chain fatty acid metabolic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0008775 - acetate CoA-transferase activity Inferred from experiment Inferred by computational analysis [GOA01, Pauli72]
GO:0008410 - CoA-transferase activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization fatty acids

Unification Links: EcoliWiki:b2222 , ModBase:P76459 , PR:PRO_000022180 , Pride:P76459 , Protein Model Portal:P76459 , RefSeq:NP_416726 , SMR:P76459 , String:511145.b2222 , UniProt:P76459

Relationship Links: InterPro:IN-FAMILY:IPR004164 , InterPro:IN-FAMILY:IPR004165 , InterPro:IN-FAMILY:IPR012791 , Panther:IN-FAMILY:PTHR13707 , Pfam:IN-FAMILY:PF01144 , Prosite:IN-FAMILY:PS01274 , Smart:IN-FAMILY:SM00882

Summary:
Based on sequence similarity, AtoA is predicted to be an acetate CoA-transferase [Reed03].

AtoA: "acetoacetate" [Pauli72]

Gene Citations: [Jenkins87]

Essentiality data for atoA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 3]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 4]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 5]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 4]
Yes [Feist07, Comment 6]

Subunit of acetoacetyl-CoA transferase: α complex

Gene: atoD Accession Numbers: EG11669 (EcoCyc), b2221, ECK2214

Subunit composition of α complex = [AtoD]2
         acetyl-CoA:acetoacetyl-CoA transferase, α subunit = AtoD

Map Position: [2,321,469 -> 2,322,131] (50.04 centisomes)
Length: 663 bp / 220 aa

Molecular Weight of Polypeptide: 23.526 kD (from nucleotide sequence), 26.5 kD (experimental) [Jenkins87a ]

GO Terms:

Biological Process: GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0019395 - fatty acid oxidation
GO:0046459 - short-chain fatty acid metabolic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0008410 - CoA-transferase activity Inferred by computational analysis [GOA01a]
GO:0008775 - acetate CoA-transferase activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: metabolism carbon utilization fatty acids

Unification Links: DIP:DIP-9191N , EcoliWiki:b2221 , Mint:MINT-1293580 , ModBase:P76458 , PR:PRO_000022183 , Protein Model Portal:P76458 , RefSeq:NP_416725 , SMR:P76458 , String:511145.b2221 , UniProt:P76458

Relationship Links: InterPro:IN-FAMILY:IPR004163 , InterPro:IN-FAMILY:IPR004165 , InterPro:IN-FAMILY:IPR012792 , Panther:IN-FAMILY:PTHR13707 , PDB:Structure:1K6D , Pfam:IN-FAMILY:PF01144 , Prosite:IN-FAMILY:PS01273 , Smart:IN-FAMILY:SM00882

Summary:
Based on sequence similarity, AtoD is predicted to be an acetate CoA-transferase [Reed03].

AtoD: "acetoacetate" [Pauli72]

Gene Citations: [Jenkins87]

Essentiality data for atoD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 3]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 4]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 5]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 4]
Yes [Feist07, Comment 6]

References

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

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

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

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."

Jenkins87: Jenkins LS, Nunn WD (1987). "Regulation of the ato operon by the atoC gene in Escherichia coli." J Bacteriol 1987;169(5);2096-102. PMID: 2883171

Jenkins87a: Jenkins LS, Nunn WD (1987). "Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system." J Bacteriol 1987;169(1);42-52. PMID: 3025185

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

Pauli72: Pauli G, Overath P (1972). "ato Operon: a highly inducible system for acetoacetate and butyrate degradation in Escherichia coli." Eur J Biochem 1972;29(3);553-62. PMID: 4563344

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

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

Sramek75: Sramek SJ, Frerman FE (1975). "Purification and properties of Escherichia coli coenzyme A-transferase." Arch Biochem Biophys 1975;171(1);14-26. PMID: 1103739

Sramek75a: Sramek SJ, Frerman FE (1975). "Escherichia coli coenzyme A-transferase: kinetics, catalytic pathway and structure." Arch Biochem Biophys 1975;171(1);27-35. PMID: 1103741

Sramek77: Sramek SJ, Frerman FE, McCormick DJ, Duncombe GR (1977). "Substrate-induced conformational changes and half-the-sites reactivity in the Escherichia coli CoA transferase." Arch Biochem Biophys 1977;181(2);525-33. PMID: 332081

UniProtGOA11: 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."


Report Errors or Provide Feedback
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 18.5 on Wed Nov 26, 2014, biocyc14.