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InterPro: IPR018294 4-diphosphocytidyl-2C-methyl-D-erythritol synthase, conserved site

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UniProtKB

Matches:

1283 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR018294 ISPD_synthase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01295	ISPD	1283
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001228 4-diphosphocytidyl-2C-methyl-D-erythritol synthase

GO Term annotation Help

Process

GO:0008299 isoprenoid biosynthetic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

4-diphosphocytidyl-2C-methyl-D-erythritol synthase, a bacterial ispD protein, catalyzes the third step of the deoxyxylulose-5-phosphate pathway (DXP) of isoprenoid biosynthesis; the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate [1]. The isoprenoid pathway is a well known target for anti-infective drug development [2, 3].

This entry represents a pattern that identifies IspD. The pattern is centred on a central conserved region that contains a conserved Asp and Arg residues.

Structural links Help

PDB - click here

SCOP: c.68.1.13

CATH: 3.90.550.10

Database links Help

Enzyme: EC:2.7.7.60

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018294

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A4D126 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein

P69834 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, chloroplastic

P74323 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Q46893 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Q5RJG7 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001228	4-diphosphocytidyl-2C-methyl-D-erythritol synthase
IPR018294	4-diphosphocytidyl-2C-methyl-D-erythritol synthase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Rohdich F, Wungsintaweekul J, Eisenreich W, Richter G, Schuhr CA, Hecht S, Zenk MH, Bacher A. Biosynthesis of terpenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase of Arabidopsis thaliana. Proc. Natl. Acad. Sci. U.S.A. 97 6451-6 2000 [PubMed: 10841550] http://dx.doi.org/10.1073/pnas.97.12.6451
2.	Illarionova V, Kaiser J, Ostrozhenkova E, Bacher A, Fischer M, Eisenreich W, Rohdich F. Nonmevalonate terpene biosynthesis enzymes as antiinfective drug targets: substrate synthesis and high-throughput screening methods. J. Org. Chem. 71 8824-34 2006 [PubMed: 17081012] http://dx.doi.org/10.1021/jo061466o
3.	Eoh H, Brown AC, Buetow L, Hunter WN, Parish T, Kaur D, Brennan PJ, Crick DC. Characterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug development. J. Bacteriol. 189 8922-7 2007 [PubMed: 17921290] http://dx.doi.org/10.1128/JB.00925-07

Additional Reading Open in usermanual
	Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP. Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis. Nat. Struct. Biol. 8 2001 641-8 [PubMed: 11427897] http://dx.doi.org/10.1038/89691
	Rohdich F, Wungsintaweekul J, Fellermeier M, Sagner S, Herz S, Kis K, Eisenreich W, Bacher A, Zenk MH. Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol. Proc. Natl. Acad. Sci. U.S.A. 96 1999 11758-63 [PubMed: 10518523] http://dx.doi.org/10.1073/pnas.96.21.11758
	Gabrielsen M, Bond CS, Hallyburton I, Hecht S, Bacher A, Eisenreich W, Rohdich F, Hunter WN. Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis. J. Biol. Chem. 279 2004 52753-61 [PubMed: 15466439] http://dx.doi.org/10.1074/jbc.M408895200
	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
	Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN. The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate. FEBS J. 273 2006 1065-73 [PubMed: 16478479] http://dx.doi.org/10.1111/j.1742-4658.2006.05133.x
	Kemp LE, Bond CS, Hunter WN. Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. Acta Crystallogr. D Biol. Crystallogr. 59 2003 607-10 [PubMed: 12595740] http://dx.doi.org/10.1107/S090744490202365X

InterPro 23.1