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MetaCyc Protein: β complex

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

Species: Escherichia coli K-12 substr. MG1655

Component of: acetoacetyl-CoA transferase (summary available)

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

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

AtoA: "acetoacetate" [Pauli72]

Locations: cytosol

Map Position: [2,322,131 -> 2,322,781]

Molecular Weight of Polypeptide: 22.96 kD (from nucleotide sequence), 26 kD (experimental) [Jenkins87 ]

Unification Links: ASAP:ABE-0007349 , CGSC:986 , EchoBASE:EB1621 , EcoGene:EG11670 , EcoliWiki:b2222 , ModBase:P76459 , OU-Microarray:b2222 , PortEco:atoA , PR:PRO_000022180 , Pride:P76459 , Protein Model Portal:P76459 , RefSeq:NP_416726 , RegulonDB:EG11670 , 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

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

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 [GOA01]
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, Arifuzzaman, 2006]
GO:0008775 - acetate CoA-transferase activity Inferred from experiment Inferred by computational analysis [GOA01a, Pauli72]
GO:0008410 - CoA-transferase activity Inferred by computational analysis [GOA01]
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

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Subunit of: acetoacetyl-CoA transferase

Species: Escherichia coli K-12 substr. MG1655

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]

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Enzymatic reaction of: acetoacetyl-CoA transferase

Synonyms: acetyl-CoA:acetoacetate-CoA transferase

EC Number: 2.8.3.-

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

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)

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

Citations: [Sramek75a]

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

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


Sequence Features

Feature Class Location Citations Comment
Active-Site 46
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;

History:
10/20/97 Gene b2222 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11670.


References

Arifuzzaman, 2006: 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

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

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.

Jenkins87: 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

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

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

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 MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sat Mar 28, 2015, BIOCYC13B.