Summary: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase Edit Wikipedia article
|2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase|
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
2c-methyl-d-erythritol 4-phosphate cytidylyltransferase (ispd) from arabidopsis thaliana
- 2-C-methyl-D-erythritol 4-phosphate + CTP diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
This enzyme participates in biosynthesis of steroids. It 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. The isoprenoid pathway is a well known target for anti-infective drug development.
The systematic name of this enzyme class is CTP:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. This enzyme is also called:
- MEP cytidylyltransferas
- CDP-ME synthetase
It is normally abbreviated IspD. It is also referenced by the open reading frame YgbP.
The crystal structure of the E. coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 1I52, 1INI & 1INJ, reported by Richard et al. (2001), was the first one for an enzyme involved in the MEP pathway.
- Rohdich F, Wungsintaweekul J, Eisenreich W, Richter G, Schuhr CA, Hecht S, Zenk MH, Bacher A (June 2000). "Biosynthesis of terpenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase of Arabidopsis thaliana". Proceedings of the National Academy of Sciences of the United States of America 97 (12): 6451–6. doi:10.1073/pnas.97.12.6451. PMC 18623. PMID 10841550.
- Illarionova V, Kaiser J, Ostrozhenkova E, Bacher A, Fischer M, Eisenreich W, Rohdich F (November 2006). "Nonmevalonate terpene biosynthesis enzymes as antiinfective drug targets: substrate synthesis and high-throughput screening methods". J. Org. Chem. 71 (23): 8824–34. doi:10.1021/jo061466o. PMID 17081012.
- Eoh H, Brown AC, Buetow L, Hunter WN, Parish T, Kaur D, Brennan PJ, Crick DC (December 2007). "Characterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug development". J. Bacteriol. 189 (24): 8922–7. doi:10.1128/JB.00925-07. PMC 2168624. PMID 17921290.
- Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP (2001). "Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis.". Nature Structural & Molecular Biology 8 (7): 641–8. doi:10.1038/89691. PMID 11427897.
- Kuzuyama T, Takagi M, Kaneda K, Dairi T and Seto H (2000). "Formation of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway". Tetrahedron Lett. 41 (50): 703–706. doi:10.1016/S0040-4039(99)02143-7.
- K, Eisenreich W, Bacher A, Zenk MH (1999). "Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol". Proceedings of the National Academy of Sciences of the United States of America 96 (21): 11758–63. doi:10.1073/pnas.96.21.11758. PMC 18359. PMID 10518523.
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase Provide feedback
Members of this family are enzymes which catalyse the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP) .
Rohdich F, Wungsintaweekul J, Fellermeier M, Sagner S, Herz S, Kis K, Eisenreich W, Bacher A, Zenk MH;, Proc Natl Acad Sci U S A. 1999;96:11758-11763.: Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol. PUBMED:10518523 EPMC:10518523
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001228
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 [PUBMED:10841550]. The isoprenoid pathway is a well known target for anti-infective drug development [PUBMED:17081012, PUBMED:17921290].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||catalytic activity (GO:0003824)|
|Biological process||isoprenoid biosynthetic process (GO:0008299)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This is the GT-A clan that contains diverse glycosyltransferases that possess a Rossmann like fold .
The clan contains the following 44 members:Anp1 Caps_synth Cellulose_synt CgtA CHGN Chitin_synth_1 Chitin_synth_2 CofC CTP_transf_3 DUF2064 DUF273 DUF604 Fringe Galactosyl_T GlcNAc Gly_transf_sug Glyco_tranf_2_2 Glyco_tranf_2_3 Glyco_tranf_2_4 Glyco_tranf_2_5 Glyco_trans_2_3 Glyco_transf_21 Glyco_transf_25 Glyco_transf_34 Glyco_transf_43 Glyco_transf_49 Glyco_transf_6 Glyco_transf_64 Glyco_transf_7C Glyco_transf_7N Glyco_transf_8 Glyco_transf_92 Glycos_transf_2 GNT-I IspD Mannosyl_trans3 MGAT2 NTP_transf_3 NTP_transferase Nucleotid_trans Pox_P35 Rhamno_transf TcdA_TcdB UDPGP
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Curation and family details
|Author:||Finn RD, Bateman A, Eberhardt R|
|Number in seed:||6|
|Number in full:||4492|
|Average length of the domain:||220.50 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||84.34 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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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 IspD domain has been found. There are 49 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 seqence.
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