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InterPro: IPR004820 Cytidylyltransferase

Protein matches Help

UniProtKB

Matches:

5566 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004820 Cytidylyltransf

Secondary

IPR001994

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01467	CTP_transf_2	5566
Signatures in BioMart

InterPro Relationships Help

Parent

IPR014729 Rossmann-like alpha/beta/alpha sandwich fold

Children

IPR001980 Coenzyme A biosynthesis protein
IPR006409 Glycerol-3-phosphate cytidylyltransferase
IPR006418 Nicotinamide-nucleotide adenylyltransferase, archaeal type
IPR011914 RfaE bifunctional protein, domain II

Found in

IPR005248 Probable nicotinate-nucleotide adenylyltransferase

Contains

IPR004821 Cytidyltransferase-related

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0016779 nucleotidyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family includes [1]:

Cholinephosphate cytidyltransferase (P49585).
Glycerol-3-phosphate cytidyltransferase (P27623).

CTP:cholinephosphate cytidylyltransferase (CCT) is a key regulatory enzyme in phosphatidylcholine biosynthesis that catalyzes the formation of CDP-choline. A comparison of the catalytic domains of CCTs from a wide variety of organisms reveals a large number of completely conserved residues. There may be a role for the conserved HXGH sequence in catalysis. The membrane-binding domain in rat CCT has been defined, and it has been suggested that lipids may play a role in inactivating the enzyme. A phosphorylation domain has been described [2].

Structural links Help

PDB - click here

SCOP: c.26.1.2 , c.26.1.3

CATH: 3.40.50.300 , 3.40.50.620

Database links Help

Enzyme: EC:2.7.7

PANDIT: PF01467

Blocks: IPB004820

Pfam Clan: CL0119.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004820

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P13259 Choline-phosphate cytidylyltransferase

P49583 Putative choline-phosphate cytidylyltransferase

Q96T66 Nicotinamide mononucleotide adenylyltransferase 3

Q9DBL7 Bifunctional coenzyme A synthase

Q9ZPV8 Phosphopantetheine adenylyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR004821	Cytidyltransferase-related
IPR004820	Cytidylyltransferase
IPR019450	Nicotinamide mononucleotide adenylyltransferase, C-terminal
IPR001977	Dephospho-CoA kinase
IPR005248	Probable nicotinate-nucleotide adenylyltransferase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Clement JM, Kent C. CTP:phosphocholine cytidylyltransferase: insights into regulatory mechanisms and novel functions. Biochem. Biophys. Res. Commun. 257 643-50 1999 [PubMed: 10208837] http://dx.doi.org/10.1006/bbrc.1999.0512
2.	Kent C. CTP:phosphocholine cytidylyltransferase. Biochim. Biophys. Acta 1348 79-90 1997 [PubMed: 9370319] http://dx.doi.org/10.1016/S0005-2760(97)00112-4

Additional Reading Open in usermanual
	Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH. Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus. Acta Crystallogr. D Biol. Crystallogr. 60 2004 97-104 [PubMed: 14684898]
	Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 60 2005 787-96 [PubMed: 16021622] http://dx.doi.org/10.1002/prot.20541
	Morris VK, Izard T. Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase. Protein Sci. 13 2004 2547-52 [PubMed: 15322293] http://dx.doi.org/10.1110/ps.04816904
	Yoon HJ, Kim HL, Mikami B, Suh SW. Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation. J. Mol. Biol. 351 2005 258-65 [PubMed: 16009375] http://dx.doi.org/10.1016/j.jmb.2005.06.001
	Fong DH, Yim VC, D'Elia MA, Brown ED, Berghuis AM. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 1764 2006 63-9 [PubMed: 16344011] http://dx.doi.org/10.1016/j.bbapap.2005.10.015

InterPro 23.1