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4  structures 8539  species 0  interactions 12518  sequences 64  architectures

Family: CTP_transf_1 (PF01148)

Summary: Cytidylyltransferase family

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This is the Wikipedia entry entitled "Phosphatidate cytidylyltransferase". More...

Phosphatidate cytidylyltransferase Edit Wikipedia article

phosphatidate cytidylyltransferase
EC number2.7.7.41
CAS number9067-83-8
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Cytidylyltransferase family
OPM superfamily414
OPM protein4q2e

Phosphatidate cytidylyltransferase (EC[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.


  1. ^ Sparrow CP, Raetz CR (1985). "Purification and properties of the membrane-bound CDP-diglyceride synthetase from Escherichia coli". J. Biol. Chem. 260 (22): 12084–12091. PMID 2995359.
  2. ^ 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): 789–795. doi:10.1074/jbc.271.2.789. PMID 8557688.
  3. ^ 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): 9503–9509. 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): 678–83. PMID 4291255.
  • McCaman RE, Finnerty WR (1968). "Biosynthesis of cytidine diphosphate-diglyceride by a particulate fracgion from Micrococcus cerificans". J. Biol. Chem. 243 (19): 5074–80. PMID 5679981.
  • Petzold GL, Agranoff BW (1967). "The biosynthesis of cytidine diphosphate diglyceride by embryonic chick brain". J. Biol. Chem. 242 (6): 1187–91. PMID 6067194.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Cytidylyltransferase family Provide feedback

The members of this family are integral membrane protein cytidylyltransferases. The family includes phosphatidate cytidylyltransferase EC: as well as Sec59 from yeast. Sec59 is a dolichol kinase EC:

Internal database links

External database links

This tab holds annotation information from the InterPro database.

No InterPro data for this Pfam family.

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

This family is a member of clan CTPT (CL0234), which has the following description:

This clan includes the integral membrane CTP transferase family as well as a large family of uncharacterised proteins that may also function as nucleotidyltransferases.

The clan contains the following 2 members:

CarS-like CTP_transf_1


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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB 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.

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Representative proteomes UniProt

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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.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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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...


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 View help on the curation process

Seed source: Pfam-B_921 (release 3.0)
Previous IDs: Cytidylyltrans;
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Bateman A
Number in seed: 34
Number in full: 12518
Average length of the domain: 268.70 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 83.74 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.0 24.0
Trusted cut-off 24.0 24.0
Noise cut-off 23.9 23.9
Model length: 265
Family (HMM) version: 23
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CTP_transf_1 domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0P0V8H0 View 3D Structure Click here
A0A0R0G822 View 3D Structure Click here
A0A0R4IMQ7 View 3D Structure Click here
A0A1D6F9C4 View 3D Structure Click here
A0A1D6GB70 View 3D Structure Click here
A0A1D6GZC8 View 3D Structure Click here
A0A1D6I1F6 View 3D Structure Click here
A0A1D6J5F3 View 3D Structure Click here
A0A1D6JZP4 View 3D Structure Click here
A0A1D6KTN0 View 3D Structure Click here
A0A1D6LIW5 View 3D Structure Click here
A0A1D8PNV9 View 3D Structure Click here
A0A2R8RZN1 View 3D Structure Click here
A2BGK0 View 3D Structure Click here
A4I295 View 3D Structure Click here
B4F883 View 3D Structure Click here
B6TI87 View 3D Structure Click here
B6TTP9 View 3D Structure Click here
B6TYH9 View 3D Structure Click here
E9AHM2 View 3D Structure Click here
I1LC78 View 3D Structure Click here
I1NI71 View 3D Structure Click here
K7KBI1 View 3D Structure Click here
K7LR27 View 3D Structure Click here
K7MQ49 View 3D Structure Click here
O04928 View 3D Structure Click here
O35052 View 3D Structure Click here
O49639 View 3D Structure Click here
O95674 View 3D Structure Click here
P0ABG1 View 3D Structure Click here
P38221 View 3D Structure Click here
P53439 View 3D Structure Click here
P56079 View 3D Structure Click here
P76091 View 3D Structure Click here
P98191 View 3D Structure Click here
P9WPF7 View 3D Structure Click here
Q1PE48 View 3D Structure Click here
Q2G1Z6 View 3D Structure Click here
Q4CVA0 View 3D Structure Click here
Q4CXV8 View 3D Structure Click here