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InterPro: IPR004821 Cytidyltransferase-related

Protein matches Help

UniProtKB

Matches:

6395 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

IPR004821 Cyt_trans_rel

Secondary

IPR001994

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00125	cyt_tran_rel	6395
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001980 Coenzyme A biosynthesis protein
IPR003721 Pantoate-beta-alanine ligase
IPR004820 Cytidylyltransferase
IPR005216 Citrate lyase ligase
IPR005248 Probable nicotinate-nucleotide adenylyltransferase
IPR006409 Glycerol-3-phosphate cytidylyltransferase
IPR006417 Nicotinamide-nucleotide adenylyltransferase
IPR006418 Nicotinamide-nucleotide adenylyltransferase, archaeal type
IPR011914 RfaE bifunctional protein, domain II
IPR013166 Citrate lyase ligase, C-terminal
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
IPR016429 Bifunctional transcriptional regulator NadR

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.

Structural links Help

PDB - click here

SCOP: c.26.1.2 , c.26.1.3 , c.26.1.4

CATH: 3.40.50.620

Database links Help

Enzyme: EC:2.7.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004821

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P13259 Choline-phosphate cytidylyltransferase

P49583 Putative choline-phosphate cytidylyltransferase

Q99447 Ethanolamine-phosphate cytidylyltransferase

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
IPR001977	Dephospho-CoA kinase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Help

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