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

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

Regulation Summary Diagram: ?

Regulation summary diagram for pgsA

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, 154°)
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: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006655 - phosphatidylglycerol biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0008654 - phospholipid biosynthetic process Inferred by computational analysis [UniProtGOA11a, 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 [UniProtGOA11a]
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 [UniProtGOA11, UniProtGOA11a, GOA06, DiazMejia09, Zhang07, Daley05]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Gopalakrishnan86]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Krogh01]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, 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:

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: superpathway of phospholipid biosynthesis I (bacteria) , cardiolipin biosynthesis III , cardiolipin biosynthesis I

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:

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

Sequence Features

Protein sequence of phosphatidylglycerophosphate synthase with features indicated

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

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b1912 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10706; confirmed by SwissProt match.


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."

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

Krogh01: Krogh A, Larsson B, von Heijne G, Sonnhammer EL (2001). "Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes." J Mol Biol 305(3);567-80. PMID: 11152613

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.

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

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 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."

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 19.0 on Wed Sep 2, 2015, biocyc12.