|Gene:||cdsA||Accession Numbers: EG10139 (EcoCyc), b0175, ECK0174|
CDP-diglyceride synthetase catalyzes the synthesis of a CDP-diacylglycerol, the activated form of a 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid). CDP-diacylglycerol is positioned at a branchpoint in the lipid biosynthetic pathway where it reacts with sn-glycerol 3-phosphate to form an L-1-phosphatidylglycerol-phosphate, or with L-serine to form an L-1-phosphatidylserine. It is the source of the phosphatidyl group for all of the major phospholipids in E. coli [KANFER64, Chang67, Carter68, Raetz73, Tunaitis73, Hirschberg72, Langley78].
The properties of both the partially purified [Langley78] and purified [Sparrow85] enzyme have been studied. Mutants in cdsA contain significantly elevated levels of a 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) in vivo [Ganong80, Ganong82, Ganong83].
Gene Citations: [Icho85]
Locations: inner membrane
|Map Position: [195,677 -> 196,534] (4.22 centisomes, 15°)||Length: 858 bp / 285 aa|
Molecular Weight of Polypeptide: 31.454 kD (from nucleotide sequence), 27.0 kD (experimental) [Sparrow85 ]
Unification Links: ASAP:ABE-0000600 , CGSC:930 , EchoBASE:EB0137 , EcoGene:EG10139 , EcoliWiki:b0175 , OU-Microarray:b0175 , PortEco:cdsA , PR:PRO_000022266 , Protein Model Portal:P0ABG1 , RefSeq:NP_414717 , RegulonDB:EG10139 , SMR:P0ABG1 , String:511145.b0175 , UniProt:P0ABG1
Instance reaction of [CTP + a 1,2-diacyl-sn-glycerol 3-phosphate + H+ → a CDP-diacylglycerol + diphosphate] (18.104.22.168):
|Biological Process:||GO:0016024 - CDP-diacylglycerol biosynthetic process
[UniProtGOA12, Ganong82, Langley78]
GO:0006629 - lipid metabolic process [UniProtGOA11]
GO:0006655 - phosphatidylglycerol biosynthetic process [Gaudet10]
GO:0008654 - phospholipid biosynthetic process [UniProtGOA11]
|Molecular Function:||GO:0004605 - phosphatidate cytidylyltransferase activity
GO:0016740 - transferase activity [UniProtGOA11]
GO:0016772 - transferase activity, transferring phosphorus-containing groups [GOA01]
GO:0016779 - nucleotidyltransferase activity [UniProtGOA11]
|Cellular Component:||GO:0005886 - plasma membrane
[UniProtGOA11a, UniProtGOA11, DiazMejia09, Daley05, Langley78]
GO:0016020 - membrane [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane [UniProtGOA11]
|MultiFun Terms:||cell structure → membrane|
|metabolism → biosynthesis of building blocks → fatty acids and phosphatidic acid|
|metabolism → biosynthesis of macromolecules (cellular constituents) → phospholipid|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||No||37||Aerobic||7||No [Baba06, Comment 1]|
Enzymatic reaction of: CTP:phosphatidate cytidyltransferase (CDP-diglyceride synthetase)
Synonyms: CTP:phosphatidic acid cytidylyltransferase, CDP-diglyceride pyrophosphorylase, CDP-diglyceride synthase, CDP diacylglycerol synthase, CDP-DAG synthase, CDP-DG synthase, phosphatide cytidylyltransferase
EC Number: 22.214.171.124
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 favored in the direction shown.
Enzymatic reaction of: CTP:2,3,4-saturated L-phosphatidate cytidylyltransferase (CDP-diglyceride synthetase)
EC Number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
The enzyme has an absolute requirement for a divalent cation, and K+ also enhanced activity [Langley78]. The catalyzed reaction is reversible in vitro [Sparrow85]. The enzyme has been shown to utilize both CTP and dCTP nucleotides in vitro, producing both CDP-diacylglycerol and dCDP-diacylglycerol. These two products also occur in vivo although their physiological significance is not known. The enzyme did not utilize ATP, UTP, dATP, dTTP or dGTP [Langley78, Ganong82].
The enzyme strikingly preferred a 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) substrates containing at least one double bond in their fatty acyl moieties. The routine assay substrate was phosphatidic acid made from egg phosphatidylcholine [Sparrow85].
|Transmembrane-Region||31 -> 51|
|Transmembrane-Region||56 -> 76|
|Transmembrane-Region||93 -> 113|
|Transmembrane-Region||121 -> 141|
|Transmembrane-Region||151 -> 171|
|Transmembrane-Region||190 -> 210|
|Transmembrane-Region||213 -> 233|
|Transmembrane-Region||264 -> 284|
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
10/20/97 Gene b0175 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10139; 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
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
Ganong80: Ganong BR, Leonard JM, Raetz CR (1980). "Phosphatidic acid accumulation in the membranes of Escherichia coli mutants defective in CDP-diglyceride synthetase." J Biol Chem 255(4);1623-9. PMID: 6243645
Ganong82: Ganong BR, Raetz CR (1982). "Massive accumulation of phosphatidic acid in conditionally lethal CDP-diglyceride synthetase mutants and cytidine auxotrophs of Escherichia coli." J Biol Chem 257(1);389-94. PMID: 6273438
Ganong83: Ganong BR, Raetz CR (1983). "pH-sensitive CDP-diglyceride synthetase mutants of Escherichia coli: phenotypic suppression by mutations at a second site." J Bacteriol 153(2);731-8. PMID: 6296051
Langley78: Langley KE, Kennedy EP (1978). "Partial purification and properties of CTP:phosphatidic acid cytidylyltransferase from membranes of Escherichia coli." J Bacteriol 1978;136(1);85-95. PMID: 30751
Raetz73: Raetz CR, Kennedy EP (1973). "Function of cytidine diphosphate-diglyceride and deoxycytidine diphosphate-diglyceride in the biogenesis of membrane lipids in Escherichia coli." J Biol Chem 248(3);1098-105. PMID: 4567788
Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293
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