Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) (CDP-ME synthase) (MEP cytidylyltransferase) (MCT)

 ISPD_ECOLI              Reviewed;         236 AA.
Q46893; Q2MA82;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 155.
RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
EC=2.7.7.60;
AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
AltName: Full=CDP-ME synthase;
AltName: Full=MEP cytidylyltransferase;
Short=MCT;
Name=ispD; Synonyms=ygbP; OrderedLocusNames=b2747, JW2717;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
CHARACTERIZATION.
STRAIN=K12 / DH5-alpha;
PubMed=10518523; DOI=10.1073/pnas.96.21.11758;
Rohdich F., Wungsintaweekul J., Fellermeier M., Sagner S., Herz S.,
Kis K., Eisenreich W., Bacher A., Zenk M.H.;
"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. 96:11758-11763(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Kuzuyama T., Takagi M., Kaneda K., Dairi T., Seto H.;
"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. 41:703-706(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
MUTAGENESIS OF THR-140 AND GLU-191.
PubMed=12859972; DOI=10.1016/S0006-291X(03)01211-7;
Sauret-Gueeto S., Ramos-Valdivia A., Ibanez E., Boronat A.,
Rodriguez-Concepcion M.;
"Identification of lethal mutations in Escherichia coli genes encoding
enzymes of the methylerythritol phosphate pathway.";
Biochem. Biophys. Res. Commun. 307:408-415(2003).
[6]
CRYSTALLIZATION.
PubMed=11468415; DOI=10.1107/S0907444901010137;
Kemp L.E., Bond C.S., Hunter W.N.;
"Crystallization and preliminary X-ray diffraction studies of
recombinant Escherichia coli 4-diphosphocytidyl-2-C-methyl-D-
erythritol synthetase.";
Acta Crystallogr. D 57:1189-1191(2001).
[7]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CTP-MG(2+) AND
IN COMPLEX WITH CDP-ME-MG(2+), AND MUTAGENESIS OF LYS-27 AND LYS-213.
STRAIN=K12;
PubMed=11427897; DOI=10.1038/89691;
Richard S.B., Bowman M.E., Kwiatkowski W., Kang I., Chow C.,
Lillo A.M., Cane D.E., Noel J.P.;
"Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase
involved in mevalonate-independent isoprenoid biosynthesis.";
Nat. Struct. Biol. 8:641-648(2001).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=12595740; DOI=10.1107/S090744490202365X;
Kemp L.E., Bond C.S., Hunter W.N.;
"Structure of a tetragonal crystal form of Escherichia coli 2-C-
methyl-D-erythritol 4-phosphate cytidylyltransferase.";
Acta Crystallogr. D 59:607-610(2003).
-!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-
methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-
phosphate (MEP).
-!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate =
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.3.;
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 2/6.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11427897}.
-!- MISCELLANEOUS: There are no coordination bonds that occur between
IspD and magnesium in any of the complexes examined to date.
-!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family.
IspD subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF230736; AAF43207.1; -; Genomic_DNA.
EMBL; AB037143; BAA90761.1; -; Genomic_DNA.
EMBL; U29579; AAA69257.1; -; Genomic_DNA.
EMBL; U00096; AAC75789.1; -; Genomic_DNA.
EMBL; AP009048; BAE76824.1; -; Genomic_DNA.
PIR; G65055; G65055.
RefSeq; NP_417227.1; NC_000913.3.
RefSeq; WP_000246138.1; NZ_LN832404.1.
PDB; 1H3M; X-ray; 2.40 A; A/B=2-236.
PDB; 1I52; X-ray; 1.50 A; A=1-236.
PDB; 1INI; X-ray; 1.82 A; A=1-236.
PDB; 1INJ; X-ray; 1.55 A; A=1-236.
PDB; 1VGT; X-ray; 1.80 A; A/B=2-236.
PDB; 1VGU; X-ray; 2.80 A; A/B=2-236.
PDB; 3N9W; X-ray; 1.90 A; A/B=2-236.
PDBsum; 1H3M; -.
PDBsum; 1I52; -.
PDBsum; 1INI; -.
PDBsum; 1INJ; -.
PDBsum; 1VGT; -.
PDBsum; 1VGU; -.
PDBsum; 3N9W; -.
ProteinModelPortal; Q46893; -.
SMR; Q46893; -.
BioGrid; 4262280; 173.
IntAct; Q46893; 2.
STRING; 316385.ECDH10B_2915; -.
DrugBank; DB03687; 4-Diphosphocytidyl-2-C-Methyl-D-Erythritol.
DrugBank; DB02431; Cytidine-5'-Triphosphate.
PaxDb; Q46893; -.
PRIDE; Q46893; -.
EnsemblBacteria; AAC75789; AAC75789; b2747.
EnsemblBacteria; BAE76824; BAE76824; BAE76824.
GeneID; 948269; -.
KEGG; ecj:JW2717; -.
KEGG; eco:b2747; -.
PATRIC; fig|1411691.4.peg.3993; -.
EchoBASE; EB2913; -.
EcoGene; EG13110; ispD.
eggNOG; ENOG4105CE5; Bacteria.
eggNOG; COG1211; LUCA.
HOGENOM; HOG000218564; -.
InParanoid; Q46893; -.
KO; K00991; -.
OMA; ERQHSVY; -.
PhylomeDB; Q46893; -.
BioCyc; EcoCyc:G7423-MONOMER; -.
BioCyc; MetaCyc:G7423-MONOMER; -.
BRENDA; 2.7.7.60; 2026.
SABIO-RK; Q46893; -.
UniPathway; UPA00056; UER00093.
EvolutionaryTrace; Q46893; -.
PRO; PR:Q46893; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
CDD; cd02516; CDP-ME_synthetase; 1.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_00108; IspD; 1.
InterPro; IPR001228; IspD.
InterPro; IPR034683; IspD/TarI.
InterPro; IPR018294; ISPD_synthase_CS.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF01128; IspD; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR00453; ispD; 1.
PROSITE; PS01295; ISPD; 1.
1: Evidence at protein level;
3D-structure; Cobalt; Complete proteome; Direct protein sequencing;
Isoprene biosynthesis; Magnesium; Manganese; Nucleotidyltransferase;
Reference proteome; Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 236 2-C-methyl-D-erythritol 4-phosphate
cytidylyltransferase.
/FTId=PRO_0000075572.
SITE 20 20 Transition state stabilizer.
{ECO:0000269|PubMed:11427897}.
SITE 27 27 Transition state stabilizer.
{ECO:0000269|PubMed:11427897}.
SITE 157 157 Positions MEP for the nucleophilic
attack. {ECO:0000269|PubMed:11427897}.
SITE 213 213 Positions MEP for the nucleophilic
attack. {ECO:0000269|PubMed:11427897}.
MUTAGEN 27 27 K->A,S: Strong decrease in activity.
{ECO:0000269|PubMed:11427897}.
MUTAGEN 140 140 T->I: Loss of activity.
{ECO:0000269|PubMed:12859972}.
MUTAGEN 191 191 E->K: Loss of activity.
{ECO:0000269|PubMed:12859972}.
MUTAGEN 213 213 K->S: Decrease in activity.
{ECO:0000269|PubMed:11427897}.
STRAND 8 14 {ECO:0000244|PDB:1I52}.
HELIX 19 21 {ECO:0000244|PDB:1I52}.
STRAND 23 25 {ECO:0000244|PDB:1INI}.
HELIX 27 29 {ECO:0000244|PDB:1I52}.
STRAND 30 32 {ECO:0000244|PDB:1I52}.
HELIX 37 46 {ECO:0000244|PDB:1I52}.
STRAND 51 58 {ECO:0000244|PDB:1I52}.
HELIX 65 67 {ECO:0000244|PDB:1I52}.
HELIX 69 72 {ECO:0000244|PDB:1I52}.
STRAND 76 80 {ECO:0000244|PDB:1I52}.
HELIX 85 94 {ECO:0000244|PDB:1I52}.
STRAND 100 104 {ECO:0000244|PDB:1I52}.
HELIX 114 121 {ECO:0000244|PDB:1I52}.
HELIX 122 125 {ECO:0000244|PDB:1I52}.
STRAND 131 136 {ECO:0000244|PDB:1I52}.
STRAND 141 144 {ECO:0000244|PDB:1I52}.
STRAND 148 155 {ECO:0000244|PDB:1I52}.
STRAND 161 170 {ECO:0000244|PDB:1I52}.
HELIX 171 183 {ECO:0000244|PDB:1I52}.
HELIX 191 197 {ECO:0000244|PDB:1I52}.
STRAND 203 206 {ECO:0000244|PDB:1I52}.
HELIX 219 227 {ECO:0000244|PDB:1I52}.
HELIX 229 233 {ECO:0000244|PDB:3N9W}.
SEQUENCE 236 AA; 25737 MW; 6AD26690AC2CF201 CRC64;
MATTHLDVCA VVPAAGFGRR MQTECPKQYL SIGNQTILEH SVHALLAHPR VKRVVIAISP
GDSRFAQLPL ANHPQITVVD GGDERADSVL AGLKAAGDAQ WVLVHDAARP CLHQDDLARL
LALSETSRTG GILAAPVRDT MKRAEPGKNA IAHTVDRNGL WHALTPQFFP RELLHDCLTR
ALNEGATITD EASALEYCGF HPQLVEGRAD NIKVTRPEDL ALAEFYLTRT IHQENT


Related products :

Catalog number Product name Quantity
ISPD_RAT Rat ELISA Kit FOR 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein 96T
ISPD_MOUSE Mouse ELISA Kit FOR 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein 96T
M304652 Methyl-D-erythritol-d3 Phosphate Disodium Salt C5H8D3Na2O7P CAS: 1 mg
M304650 Methyl-D-erythritol Phosphate Disodium Salt C5H11Na2O7P CAS: 270928-69-3 1 mg
EIAAB06601 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,Homo sapiens,Human
EIAAB06600 Bos taurus,Bovine,CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,
EIAAB06599 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,Cds,CDS 1,Cds1,CTP phosphatidate cytidylyltransferase 1,Mouse,Mus musc
EIAAB06603 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Mouse,Mus musculus
EIAAB06597 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,CDS,CDS 1,CDS1,CTP phosphatidate cytidylyltransferase 1,Homo sapiens,H
EIAAB26969 Bos taurus,Bovine,CMAS,CMP-N-acetylneuraminic acid synthase,CMP-NeuNAc synthase,N-acylneuraminate cytidylyltransferase
EIAAB26968 Cmas,CMP-N-acetylneuraminic acid synthase,CMP-NeuNAc synthase,Mouse,Mus musculus,N-acylneuraminate cytidylyltransferase
EIAAB26970 Cmas,CMP-N-acetylneuraminic acid synthase,CMP-NeuNAc synthase,N-acylneuraminate cytidylyltransferase,Rat,Rattus norvegicus
EIAAB06602 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Phosphatidate cyti
EIAAB26967 CMAS,CMP-N-acetylneuraminic acid synthase,CMP-NeuNAc synthase,Homo sapiens,Human,N-acylneuraminate cytidylyltransferase
EIAAB30232 CTP phosphoethanolamine cytidylyltransferase,Ethanolamine-phosphate cytidylyltransferase,Mouse,Mus musculus,Pcyt2,Phosphorylethanolamine transferase
EIAAB30231 Bos taurus,Bovine,CTP phosphoethanolamine cytidylyltransferase,Ethanolamine-phosphate cytidylyltransferase,PCYT2,Phosphorylethanolamine transferase
EIAAB30233 CTP phosphoethanolamine cytidylyltransferase,Ethanolamine-phosphate cytidylyltransferase,Pcyt2,Phosphorylethanolamine transferase,Rat,Rattus norvegicus
EIAAB30234 CTP phosphoethanolamine cytidylyltransferase,Ethanolamine-phosphate cytidylyltransferase,Homo sapiens,Human,PCYT2,Phosphorylethanolamine transferase
EIAAB30228 CCT B,CCT-beta,Choline-phosphate cytidylyltransferase B,CT B,CTP phosphocholine cytidylyltransferase B,Mouse,Mus musculus,Pcyt1b,Phosphorylcholine transferase B
054892 Erythritol extrapure for biochemistry (Erythrite, meso-Erythritol) 25 g
054892 Erythritol extrapure for biochemistry (Erythrite, meso-Erythritol) 5 g
EIAAB30230 CCT B,Cctb,CCT-beta,Choline-phosphate cytidylyltransferase B,CT B,CTP phosphocholine cytidylyltransferase B,Pcyt1b,Phosphorylcholine transferase B,Rat,Rattus norvegicus
EIAAB30227 CCT A,CCT-alpha,Choline-phosphate cytidylyltransferase A,CT A,CTP phosphocholine cytidylyltransferase A,Ctpct,Pcyt1,Pcyt1a,Phosphorylcholine transferase A,Rat,Rattus norvegicus
EIAAB30229 CCT B,CCTB,CCT-beta,Choline-phosphate cytidylyltransferase B,CT B,CTP phosphocholine cytidylyltransferase B,Homo sapiens,Human,PCYT1B,Phosphorylcholine transferase B
EIAAB30225 CCT A,CCT-alpha,Choline-phosphate cytidylyltransferase A,CT A,CTP phosphocholine cytidylyltransferase A,Ctpct,Mouse,Mus musculus,Pcyt1,Pcyt1a,Phosphorylcholine transferase A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur