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MetaCyc Enzyme: 2-acylglycerophosphoethanolamine acyltransferase / acyl-ACP synthetase

Gene: aas Accession Numbers: EG11679 (MetaCyc), b2836, ECK2832

Species: Escherichia coli K-12 substr. MG1655

Summary:
The protein contains bound ACP. [Hsu91, Cooper89]

Based on sequence similarity, Aas has been predicted to be a hydroxycinnamate-CoA ligase [Reed03].

Locations: inner membrane

Map Position: [2,971,877 <- 2,974,036]

Molecular Weight of Polypeptide: 80.7 kD (from nucleotide sequence)

pI: 9.37

Unification Links: ASAP:ABE-0009302 , CGSC:29780 , DIP:DIP-9025N , EchoBASE:EB1630 , EcoGene:EG11679 , EcoliWiki:b2836 , Mint:MINT-1308806 , ModBase:P31119 , OU-Microarray:b2836 , PortEco:aas , PR:PRO_000022025 , Protein Model Portal:P31119 , RefSeq:NP_417313 , RegulonDB:EG11679 , SMR:P31119 , String:511145.b2836 , UniProt:P31119

Relationship Links: InterPro:IN-FAMILY:IPR000873 , InterPro:IN-FAMILY:IPR002123 , InterPro:IN-FAMILY:IPR020845 , InterPro:IN-FAMILY:IPR023775 , Pfam:IN-FAMILY:PF00501 , Pfam:IN-FAMILY:PF01553 , Prosite:IN-FAMILY:PS00455 , Smart:IN-FAMILY:SM00563

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006631 - fatty acid metabolic process Inferred from experiment Inferred by computational analysis [GOA01a, Hsu91]
GO:0008654 - phospholipid biosynthetic process Inferred from experiment Inferred by computational analysis [GOA01a, Hsu91]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0008779 - acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Rock79]
GO:0008922 - long-chain fatty acid [acyl-carrier-protein] ligase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Rock79]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, DiazMejia09, Zhang07]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Rock79]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
information transfer protein related posttranslational modification
metabolism biosynthesis of building blocks fatty acids and phosphatidic acid
regulation type of regulation unknown

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: acyl-ACP synthetase

octanoate + a holo-[acyl-carrier protein] + ATP <=> an octanoyl-[acp] + AMP + diphosphate

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

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 2-acylglycerophosphoethanolamine acyltransferase

Synonyms: 2-acyl-GPE acyltransferase, acyl-[acyl-carrier protein]-phospholipid O-acyltransferase, acyl-[acyl-carrier protein]:O-(acyl-sn-glycero-3-phospho)-ethanolamine O-acyltransferase

EC Number: 2.3.1.40

an acyl-[acyl-carrier protein] + a 1-lyso-2-acyl-sn-glycero-3-phosphoethanolamine <=> a holo-[acyl-carrier protein] + an L-1-phosphatidyl-ethanolamine

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]:

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
2-Acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase and acyl-acyl carrier protein (acyl-ACP) synthetase are dual catalytic activities encoded by the aas gene. Both enzymes participate in membrane phospholipid turnover and the uptake and incorporation of exogenous 2-acyllysophospholipids. The function of 2-acyl-GPE acyltransferase is to regenerate phosphatidylethanolamine (PtdEtn) from 2-acyl-GPE formed by transacylation reactions or phospholipase A1 action. In the process enzyme-bound ACP is also regenerated. [Jackowski94, Hsu91]

Cofactors or Prosthetic Groups: Mg2+ [Rock84]

Inhibitors (Unknown Mechanism): Li+ [Comment 2]


Enzymatic reaction of: acyl-ACP synthetase

Synonyms: acyl-acyl carrier protein synthetase, long chain fatty acid-[acyl-carrier protein] ligase, long chain fatty acid-[acyl-carrier protein] ligase (AMP-forming)

ATP + a holo-[acyl-carrier protein] + a fatty acid <=> AMP + a 2,3,4-saturated fatty acyl-[acp] + diphosphate

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

The reaction is physiologically favored in the direction shown.

Alternative Substrates [Comment 3]:

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
2-Acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase and acyl-acyl carrier protein (acyl-ACP) synthetase are dual catalytic activities encoded by the aas gene. Both enzymes participate in membrane phospholipid turnover and the uptake and incorporation of exogenous 2-acyllysophospholipids. Acyl-ACP synthetase functions to ligate free fatty acids, with lengths of C-8 to C-18, to ACP. [Jackowski94, Hsu91, Rock79]

Cofactors or Prosthetic Groups: Mg2+ [Comment 4]

Inhibitors (Unknown Mechanism): a salt


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 15 -> 16
[Jackowski94, UniProt10]
Alternate sequence: AL; UniProt: (in Ref. 1; AAA17550);
Protein-Segment 15 -> 138
[UniProt10a]
UniProt: Acyltransferase; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 36
[Heath98, UniProt11]
Alternate sequence: A; UniProt: Loss of 2-acyl-GPE acyltransferase activity; retains acyl-ACP synthetase activity.
Active-Site 36
[UniProt10]
Sequence-Conflict 202
[Jackowski94, UniProt10]
Alternate sequence: S; UniProt: (in Ref. 1; AAA17550);
Protein-Segment 233 -> 646
[UniProt10a]
UniProt: AMP-binding; Sequence Annotation Type: region of interest;
Transmembrane-Region 258 -> 277
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 281
[Lenski03, UniProt10]
Alternate sequence: I; UniProt: (in Ref. 4; AAT42454);
Transmembrane-Region 409 -> 433
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;

History:
10/20/97 Gene b2836 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11679; confirmed by SwissProt match.


References

Cooper89: Cooper CL, Hsu L, Jackowski S, Rock CO (1989). "2-Acylglycerolphosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase is a membrane-associated acyl carrier protein binding protein." J Biol Chem 1989;264(13);7384-9. PMID: 2540190

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, 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."

Heath98: Heath RJ, Rock CO (1998). "A conserved histidine is essential for glycerolipid acyltransferase catalysis." J Bacteriol 180(6);1425-30. PMID: 9515909

Hsu91: Hsu L, Jackowski S, Rock CO (1991). "Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity." J Biol Chem 1991;266(21);13783-8. PMID: 1649829

Jackowski94: Jackowski S, Jackson PD, Rock CO (1994). "Sequence and function of the aas gene in Escherichia coli." J Biol Chem 1994;269(4);2921-8. PMID: 8300626

Lenski03: Lenski RE, Winkworth CL, Riley MA (2003). "Rates of DNA sequence evolution in experimental populations of Escherichia coli during 20,000 generations." J Mol Evol 56(4);498-508. PMID: 12664169

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

Rock79: Rock CO, Cronan JE (1979). "Solubilization, purification, and salt activation of acyl-acyl carrier protein synthetase from Escherichia coli." J Biol Chem 1979;254(15);7116-22. PMID: 378999

Rock84: Rock CO (1984). "Turnover of fatty acids in the 1-position of phosphatidylethanolamine in Escherichia coli." J Biol Chem 1984;259(10);6188-94. PMID: 6373752

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 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."

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111


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 18.5 on Sun Feb 1, 2015, BIOCYC14B.