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Escherichia coli K-12 substr. MG1655 Enzyme: phosphatidylglycerophosphate synthase



Gene: pgsA Accession Numbers: EG10706 (EcoCyc), b1912, ECK1911

Regulation Summary Diagram: ?

Summary:
Phosphatidylglycerophosphate (PGP) synthase catalyzes the committed step in the biosynthesis of acidic phospholipids. PGP synthase is an integral membrane protein tightly associated with the cytoplasmic membrane [Hirabayashi76, Gopalakrishnan86, Dowhan92].

A pgsA null E. coli strain exhibits relatively normal cell division and shows elevated amounts of phospholipid precursors and the normally minimal phospholipid N-acylphosphatidylethanolamine (N-acyl-PE) [Mileykovskaya09]

Locations: inner membrane

Map Position: [1,990,293 <- 1,990,841] (42.9 centisomes)
Length: 549 bp / 182 aa

Molecular Weight of Polypeptide: 20.701 kD (from nucleotide sequence)

pI: 10.5

Unification Links: ASAP:ABE-0006367 , CGSC:405 , EchoBASE:EB0700 , EcoGene:EG10706 , EcoliWiki:b1912 , OU-Microarray:b1912 , PortEco:pgsA , PR:PRO_000023527 , Protein Model Portal:P0ABF8 , RefSeq:NP_416422 , RegulonDB:EG10706 , String:511145.b1912 , UniProt:P0ABF8

Relationship Links: InterPro:IN-FAMILY:IPR000462 , InterPro:IN-FAMILY:IPR004570 , InterPro:IN-FAMILY:IPR023762 , Pfam:IN-FAMILY:PF01066 , Prosite:IN-FAMILY:PS00379

In Paralogous Gene Group: 290 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006655 - phosphatidylglycerol biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0008654 - phospholipid biosynthetic process Inferred by computational analysis [UniProtGOA11, GOA06, GOA01a]
Molecular Function: GO:0008444 - CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Inferred by computational analysis [GOA06, GOA01, GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016780 - phosphotransferase activity, for other substituted phosphate groups Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, DiazMejia09, Zhang07, Daley05]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, Gopalakrishnan86]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01a]

MultiFun Terms: cell structure membrane
metabolism biosynthesis of macromolecules (cellular constituents) phospholipid

Essentiality data for pgsA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Enzymatic reaction of: phosphatidylglycerophosphate synthase

Synonyms: PGP synthase, CDPdiacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase, glycerophosphate phosphatidyltransferase, 3-phosphatidyl-1'-glycerol-3'-phosphate synthase, CDPdiacylglycerol:sn-glycerol-3-phosphate 3-phosphatidyltransferase

EC Number: 2.7.8.5

a CDP-diacylglycerol + sn-glycerol 3-phosphate <=> CMP + an L-1-phosphatidylglycerol-phosphate + H+

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 for a CDP-diacylglycerol: UDP-diglyceride [Raetz78 ] , ADP-diglyceride [Raetz78 ]

Alternative Substrates for sn-glycerol 3-phosphate: 3,4,-dihydroxybutylphosphonate [Raetz78 ]

In Pathways: phospholipid biosynthesis I , cardiolipin biosynthesis III , cardiolipin biosynthesis I

Summary:
High concentrations of CDP-diacylglycerol inhibit the reaction. The reaction proceeds through an ordered sequential Bi-Bi mechanism [Hirabayashi76, Gopalakrishnan86, Dowhan92].

Cofactors or Prosthetic Groups: Mg2+ [Comment 2]

Inhibitors (Competitive): L-glyceraldehyde 3-phosphate [Tang77]

Inhibitors (Uncompetitive): a CDP-diacylglycerol [Hirabayashi76]

Inhibitors (Unknown Mechanism): Ca2+ [Hirabayashi76] , a CDP-diacylglycerol , sn-glycerol 3-phosphate [Comment 3]

Kinetic Parameters:

Substrate
Km (μM)
Citations
sn-glycerol 3-phosphate
320.0
[Dowhan92, BRENDA14]
a CDP-diacylglycerol
46.0
[Hirabayashi76, BRENDA14]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[UniProt10]
UniProt: Removed; Non-Experimental Qualifier: probable;
Chain 2 -> 182
[UniProt09]
UniProt: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
Transmembrane-Region 14 -> 38
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 60
[UniProt10a]
Alternate sequence: T → P; UniProt: In pgsA3; lower activity;
Transmembrane-Region 62 -> 82
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 88 -> 108
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 92
[UniProt10a]
Alternate sequence: T → I; UniProt: In pgsA10; lower activity;
Transmembrane-Region 147 -> 169
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1912 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10706; 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

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

Dowhan92: Dowhan W (1992). "Phosphatidylglycerophosphate synthase from Escherichia coli." Methods Enzymol 1992;209;313-21. PMID: 1323047

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."

Gopalakrishnan86: Gopalakrishnan AS, Chen YC, Temkin M, Dowhan W (1986). "Structure and expression of the gene locus encoding the phosphatidylglycerophosphate synthase of Escherichia coli." J Biol Chem 1986;261(3);1329-38. PMID: 3003065

Hirabayashi76: Hirabayashi T, Larson TJ, Dowhan W (1976). "Membrane-associated phosphatidylglycerophosphate synthetase from Escherichia coli: purification by substrate affinity chromatography on cytidine 5'-diphospho-1,2-diacyl-sn-glycerol sepharose." Biochemistry 1976;15(24);5205-11. PMID: 793612

Mileykovskaya09: Mileykovskaya E, Ryan AC, Mo X, Lin CC, Khalaf KI, Dowhan W, Garrett TA (2009). "Phosphatidic acid and N-acylphosphatidylethanolamine form membrane domains in Escherichia coli mutant lacking cardiolipin and phosphatidylglycerol." J Biol Chem 284(5);2990-3000. PMID: 19049984

Raetz78: Raetz CR (1978). "Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli." Microbiol Rev 1978;42(3);614-59. PMID: 362151

Tang77: Tang CT, Engel R, Tropp BE (1977). "L-Glyceraldehude 3-phosphate, a bactericidal agent." Antimicrob Agents Chemother 11(1);147-53. PMID: 319747

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

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

Other References Related to Gene Regulation

Zaslaver06: Zaslaver A, Bren A, Ronen M, Itzkovitz S, Kikoin I, Shavit S, Liebermeister W, Surette MG, Alon U (2006). "A comprehensive library of fluorescent transcriptional reporters for Escherichia coli." Nat Methods 3(8);623-8. PMID: 16862137


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 Sat Dec 20, 2014, BIOCYC14A.