Summary: Cytidylyltransferase family
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This is the Wikipedia entry entitled "Phosphatidate cytidylyltransferase". More...
Phosphatidate cytidylyltransferase Edit Wikipedia article
| phosphatidate cytidylyltransferase | |||||||
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| Identifiers | |||||||
| EC number | 2.7.7.41 | ||||||
| CAS number | 9067-83-8 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | CTP_transf_1 | ||||||||
| Pfam | PF01148 | ||||||||
| InterPro | IPR000374 | ||||||||
| PROSITE | PDOC01019 | ||||||||
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Phosphatidate cytidylyltransferase (EC 2.7.7.41)[1][2][3] (also known as CDP- diacylglycerol synthase) (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from cytidine triphosphate and phosphatidate.
- CTP + phosphatidate
diphosphate + CDP-diacylglycerol
Thus, the two substrates of this enzyme are cytidine triphosphate, or CTP, and phosphatidate, whereas its two products are diphosphate and CDP-diacylglycerol.
CDP-diacylglycerol is an important branch point intermediate in both prokaryotic and eukaryotic organisms. CDS is a membrane-bound enzyme.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:phosphatidate cytidylyltransferase. Other names in common use include CDP diglyceride pyrophosphorylase, CDP-diacylglycerol synthase, CDP-diacylglyceride synthetase, cytidine diphosphoglyceride pyrophosphorylase, phosphatidate cytidyltransferase, phosphatidic acid cytidylyltransferase, CTP:1,2-diacylglycerophosphate-cytidyl transferase, CTP-diacylglycerol synthetase, DAG synthetase, and CDP-DG. This enzyme participates in glycerophospholipid metabolism and phosphatidylinositol signaling system.
[edit] References
- ^ Sparrow CP, Raetz CR (1985). "Purification and properties of the membrane-bound CDP-diglyceride synthetase from Escherichia coli". J. Biol. Chem. 260 (22): 1208412091. PMID 2995359.
- ^ Shen H, Heacock PN, Clancey CJ, Dowhan W (1996). "The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth". J. Biol. Chem. 271 (2): 789795. doi:10.1074/jbc.271.2.789. PMID 8557688.
- ^ Kondo H, Goto K, Saito S, Tonosaki A (1997). "Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain". J. Biol. Chem. 272 (14): 95039509. doi:10.1074/jbc.272.14.9503. PMID 9083091.
- Carter JR, Kennedy EP (1966). "Enzymatic synthesis of cytidine diphosphate diglyceride". J. Lipid. Res. 7 (5): 67883. PMID 4291255.
- McCaman RE, Finnerty WR (1968). "Biosynthesis of cytidine diphosphate-diglyceride by a particulate fracgion from Micrococcus cerificans". J. Biol. Chem. 243 (19): 507480. PMID 5679981.
- Petzold GL, Agranoff BW (1967). "The biosynthesis of cytidine diphosphate diglyceride by embryonic chick brain". J. Biol. Chem. 242 (6): 118791. PMID 6067194.
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Cytidylyltransferase family Provide feedback
The members of this family are integral membrane protein cytidylyltransferases. The family includes phosphatidate cytidylyltransferase EC:2.7.7.41 as well as Sec59 from yeast. Sec59 is a dolichol kinase EC:2.7.1.108.
Internal database links
| Similarity to PfamA using HHSearch: | DUF46 |
External database links
| PANDIT: | PF01148 |
| PROSITE: | PDOC01019 |
| Pseudofam: | PF01148 |
| SYSTERS: | CTP_transf_1 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000374
Phosphatidate cytidylyltransferase (EC) [PUBMED:2995359, PUBMED:8557688, PUBMED:9083091] (also known as CDP- diacylglycerol synthase) (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from CTP and phosphatidate (PA):Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | membrane (GO:0016020) |
| Molecular function | transferase activity, transferring phosphorus-containing groups (GO:0016772) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (48) |
Full (6283) |
Representative proteomes | NCBI (4702) |
Meta (2431) |
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| RP15 (615) |
RP35 (1145) |
RP55 (1531) |
RP75 (1821) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Format an alignment
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (48) |
Full (6283) |
Representative proteomes | NCBI (4702) |
Meta (2431) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (615) |
RP35 (1145) |
RP55 (1531) |
RP75 (1821) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_921 (release 3.0) |
| Previous IDs: | Cytidylyltrans; |
| Type: | Family |
| Author: | Finn RD, Bateman A |
| Number in seed: | 48 |
| Number in full: | 6283 |
| Average length of the domain: | 255.40 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 86.77 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 259 | ||||||||||||
| Family (HMM) version: | 15 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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diphosphate + CDP-diacylglycerol
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence