Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: 2-acylglycerophosphoethanolamine acyltransferase / acyl-ACP synthetase



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

Regulation Summary Diagram: ?

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] (64.05 centisomes)
Length: 2160 bp / 719 aa

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

In Paralogous Gene Group: 13 (9 members) , 462 (2 members)

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

Essentiality data for aas knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
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: acyl-ACP synthetase

EC Number: 6.2.1.20

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.


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 5]:

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 6]


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)

EC Number: 6.2.1.20

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 7]:

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 8]

Inhibitors (Unknown Mechanism): a salt


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 15 -> 16
[Jackowski94, UniProt10]
Alternate sequence: RV → AL; UniProt: (in Ref. 1; AAA17550);
Protein-Segment 15 -> 138
[UniProt10b]
UniProt: Acyltransferase; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 36
[Heath98, UniProt11]
Alternate sequence: H → 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: P → S; UniProt: (in Ref. 1; AAA17550);
Protein-Segment 233 -> 646
[UniProt10b]
UniProt: AMP-binding; Sequence Annotation Type: region of interest;
Transmembrane-Region 258 -> 277
[UniProt10b]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 281
[Lenski03, UniProt10]
Alternate sequence: M → I; UniProt: (in Ref. 4; AAT42454);
Transmembrane-Region 409 -> 433
[UniProt10b]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

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


References

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

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

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."

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

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

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.

UniProt10b: 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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC13A.