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Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC 2.5.1.31) (Ditrans,polycis-undecaprenylcistransferase) (Undecaprenyl diphosphate synthase) (UDS) (Undecaprenyl pyrophosphate synthase) (UPP synthase)

 UPPS_ECOLI              Reviewed;         253 AA.
P60472; P75668; Q47675; Q9R2E4;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
16-FEB-2004, sequence version 1.
25-OCT-2017, entry version 125.
RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific);
EC=2.5.1.31;
AltName: Full=Ditrans,polycis-undecaprenylcistransferase;
AltName: Full=Undecaprenyl diphosphate synthase;
Short=UDS;
AltName: Full=Undecaprenyl pyrophosphate synthase;
Short=UPP synthase;
Name=ispU; Synonyms=rth, uppS, yaeS; OrderedLocusNames=b0174, JW0169;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
4.0 - 6.0 min (189,987 - 281,416bp) region.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[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]
CHARACTERIZATION.
PubMed=9882662;
Apfel C.M., Takacs B., Fountoulakis M., Stieger M., Keck W.;
"Use of genomics to identify bacterial undecaprenyl pyrophosphate
synthetase: cloning, expression, and characterization of the essential
uppS gene.";
J. Bacteriol. 181:483-492(1999).
[6]
CHARACTERIZATION.
PubMed=10217761;
Kato J., Fujisaki S., Nakajima K., Nishimura Y., Sato M., Nakano A.;
"The Escherichia coli homologue of yeast RER2, a key enzyme of
dolichol synthesis, is essential for carrier lipid formation in
bacterial cell wall synthesis.";
J. Bacteriol. 181:2733-2738(1999).
[7]
MUTAGENESIS OF ASP-26; GLU-73; ASP-150; ASP-190; GLU-198; GLU-213;
ASP-218 AND ASP-223.
PubMed=11076526; DOI=10.1021/bi001226h;
Pan J.-J., Yang L.-W., Liang P.-H.;
"Effect of site-directed mutagenesis of the conserved aspartate and
glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis.";
Biochemistry 39:13856-13861(2000).
[8]
MUTAGENESIS OF TRP-31; TRP-75; TRP-91; TRP-149; TRP-207 AND TRP-221.
PubMed=11744728; DOI=10.1074/jbc.M110014200;
Chen Y.-H., Chen A.P.-C., Chen C.-T., Wang A.H.-J., Liang P.-H.;
"Probing the conformational change of Escherichia coli undecaprenyl
pyrophosphate synthase during catalysis using an inhibitor and
tryptophan mutants.";
J. Biol. Chem. 277:7369-7376(2002).
[9]
REACTION MECHASNISM.
PubMed=20828539; DOI=10.1016/j.bbrc.2010.09.001;
Lu Y.P., Liu H.G., Teng K.H., Liang P.H.;
"Mechanism of cis-prenyltransferase reaction probed by substrate
analogues.";
Biochem. Biophys. Res. Commun. 400:758-762(2010).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-240, MUTAGENESIS OF
ILE-62; ALA-69; SER-71; GLU-73; ASN-74; TRP-75; ARG-77; GLU-81;
HIS-103; VAL-105; LEU-137 AND ALA-143, AND SUBUNIT.
PubMed=11581264; DOI=10.1074/jbc.M106747200;
Ko T.-P., Chen Y.-K., Robinson H., Tsai P.-C., Gao Y.-G.,
Chen A.P.-C., Wang A.H.-J., Liang P.-H.;
"Mechanism of product chain length determination and the role of a
flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase
catalysis.";
J. Biol. Chem. 276:47474-47482(2001).
[11]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 13-240 IN COMPLEX WITH
SUBSTRATES ANALOGS AND MAGNESIUM IONS, FUNCTION AS AN UNDECAPRENYL
DIPHOSPHATE SYNTHASE, MUTAGENESIS OF HIS-43; HIS-199 AND GLU-213,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
PubMed=12756244; DOI=10.1074/jbc.M302687200;
Chang S.-Y., Ko T.-P., Liang P.-H., Wang A.H.-J.;
"Catalytic mechanism revealed by the crystal structure of undecaprenyl
pyrophosphate synthase in complex with sulfate, magnesium, and
triton.";
J. Biol. Chem. 278:29298-29307(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
COFACTOR, AND SUBUNIT.
PubMed=15044730; DOI=10.1110/ps.03519904;
Chang S.Y., Ko T.P., Chen A.P., Wang A.H., Liang P.H.;
"Substrate binding mode and reaction mechanism of undecaprenyl
pyrophosphate synthase deduced from crystallographic studies.";
Protein Sci. 13:971-978(2004).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF WILD-TYPE AND OF MUTANT
ALA-26 IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS.
PubMed=15788389; DOI=10.1074/jbc.M502121200;
Guo R.T., Ko T.P., Chen A.P., Kuo C.J., Wang A.H., Liang P.H.;
"Crystal structures of undecaprenyl pyrophosphate synthase in complex
with magnesium, isopentenyl pyrophosphate, and farnesyl
thiopyrophosphate: roles of the metal ion and conserved residues in
catalysis.";
J. Biol. Chem. 280:20762-20774(2005).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS, ENZYME REGULATION, AND SUBUNIT.
PubMed=17535895; DOI=10.1073/pnas.0702254104;
Guo R.-T., Cao R., Liang P.-H., Ko T.-P., Chang T.-H., Hudock M.P.,
Jeng W.-Y., Chen C.K.-M., Zhang Y., Song Y., Kuo C.-J., Yin F.,
Oldfield E., Wang A.H.-J.;
"Bisphosphonates target multiple sites in both cis- and trans-
prenyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10022-10027(2007).
[15]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
PubMed=21294851; DOI=10.1111/j.1747-0285.2011.01101.x;
Sinko W., de Oliveira C., Williams S., Van Wynsberghe A.,
Durrant J.D., Cao R., Oldfield E., McCammon J.A.;
"Applying molecular dynamics simulations to identify rarely sampled
ligand-bound conformational states of undecaprenyl pyrophosphate
synthase, an antibacterial target.";
Chem. Biol. Drug Des. 77:412-420(2011).
-!- FUNCTION: Generates ditrans,octacis-undecaprenyl pyrophosphate
(UPP) from isopentenyl pyrophosphate (IPP) and farnesyl
diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid
in the biosynthesis of bacterial cell wall polysaccharide
components such as peptidoglycan and lipopolysaccharide.
{ECO:0000269|PubMed:12756244}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + 8 isopentenyl
diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl
diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12756244,
ECO:0000269|PubMed:15044730};
Note=Binds 2 magnesium ions per subunit.
{ECO:0000269|PubMed:12756244, ECO:0000269|PubMed:15044730};
-!- ENZYME REGULATION: Inhibited by bisphosphonates.
{ECO:0000269|PubMed:17535895}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.4 uM for FPP (at pH 7.5 and at 25 degrees Celsius)
{ECO:0000269|PubMed:12756244};
KM=4.1 uM for IPP (at pH 7.5 and at 25 degrees Celsius)
{ECO:0000269|PubMed:12756244};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11581264,
ECO:0000269|PubMed:12756244, ECO:0000269|PubMed:15044730,
ECO:0000269|PubMed:15788389, ECO:0000269|PubMed:17535895,
ECO:0000269|PubMed:21294851}.
-!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB08603.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U70214; AAB08603.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73285.1; -; Genomic_DNA.
EMBL; AP009048; BAA77849.2; -; Genomic_DNA.
PIR; F64741; F64741.
RefSeq; NP_414716.1; NC_000913.3.
RefSeq; WP_000979579.1; NZ_LN832404.1.
PDB; 1JP3; X-ray; 1.80 A; A/B=1-253.
PDB; 1UEH; X-ray; 1.73 A; A/B=1-253.
PDB; 1V7U; X-ray; 2.35 A; A/B=1-253.
PDB; 1X06; X-ray; 1.90 A; A=1-253.
PDB; 1X07; X-ray; 2.20 A; A=1-253.
PDB; 1X08; X-ray; 1.90 A; A=1-253.
PDB; 1X09; X-ray; 1.87 A; A=1-253.
PDB; 2E98; X-ray; 1.90 A; A/B=1-253.
PDB; 2E99; X-ray; 2.00 A; A/B=1-253.
PDB; 2E9A; X-ray; 2.10 A; A/B=1-253.
PDB; 2E9C; X-ray; 2.05 A; A/B=1-253.
PDB; 2E9D; X-ray; 2.50 A; A/B=1-253.
PDB; 3QAS; X-ray; 1.70 A; A/B=1-253.
PDB; 3SGV; X-ray; 1.61 A; A/B=1-253.
PDB; 3SGX; X-ray; 2.45 A; A/B=1-253.
PDB; 3SH0; X-ray; 1.84 A; A/B=1-253.
PDB; 3TH8; X-ray; 2.11 A; A/B=1-253.
PDB; 3WYJ; X-ray; 2.10 A; A/B=1-253.
PDB; 4H2J; X-ray; 1.81 A; A/B=1-253.
PDB; 4H2M; X-ray; 1.78 A; A/B=1-253.
PDB; 4H2O; X-ray; 2.14 A; A/B=1-253.
PDB; 4H38; X-ray; 1.95 A; A/B=1-253.
PDB; 4H3A; X-ray; 1.98 A; A/B=1-253.
PDB; 4H3C; X-ray; 1.93 A; A/B=1-253.
PDB; 5CQB; X-ray; 2.20 A; A/B=2-253.
PDB; 5CQJ; X-ray; 2.15 A; A/B=1-253.
PDBsum; 1JP3; -.
PDBsum; 1UEH; -.
PDBsum; 1V7U; -.
PDBsum; 1X06; -.
PDBsum; 1X07; -.
PDBsum; 1X08; -.
PDBsum; 1X09; -.
PDBsum; 2E98; -.
PDBsum; 2E99; -.
PDBsum; 2E9A; -.
PDBsum; 2E9C; -.
PDBsum; 2E9D; -.
PDBsum; 3QAS; -.
PDBsum; 3SGV; -.
PDBsum; 3SGX; -.
PDBsum; 3SH0; -.
PDBsum; 3TH8; -.
PDBsum; 3WYJ; -.
PDBsum; 4H2J; -.
PDBsum; 4H2M; -.
PDBsum; 4H2O; -.
PDBsum; 4H38; -.
PDBsum; 4H3A; -.
PDBsum; 4H3C; -.
PDBsum; 5CQB; -.
PDBsum; 5CQJ; -.
DisProt; DP00516; -.
ProteinModelPortal; P60472; -.
SMR; P60472; -.
BioGrid; 4260767; 393.
DIP; DIP-48251N; -.
IntAct; P60472; 4.
STRING; 316385.ECDH10B_0154; -.
DrugBank; DB07410; [2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACID.
DrugBank; DB07780; FARNESYL DIPHOSPHATE.
DrugBank; DB04695; FARNESYL THIOPYROPHOSPHATE.
DrugBank; DB04714; ISOPENTENYL PYROPHOSPHATE.
PaxDb; P60472; -.
PRIDE; P60472; -.
EnsemblBacteria; AAC73285; AAC73285; b0174.
EnsemblBacteria; BAA77849; BAA77849; BAA77849.
GeneID; 944874; -.
KEGG; ecj:JW0169; -.
KEGG; eco:b0174; -.
PATRIC; fig|511145.12.peg.180; -.
EchoBASE; EB3113; -.
EcoGene; EG13329; ispU.
eggNOG; ENOG4105CR3; Bacteria.
eggNOG; COG0020; LUCA.
HOGENOM; HOG000006054; -.
InParanoid; P60472; -.
KO; K00806; -.
PhylomeDB; P60472; -.
BioCyc; EcoCyc:UPPSYN-MONOMER; -.
BioCyc; MetaCyc:UPPSYN-MONOMER; -.
BRENDA; 2.5.1.31; 2026.
EvolutionaryTrace; P60472; -.
PRO; PR:P60472; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0043164; P:Gram-negative-bacterium-type cell wall biogenesis; IMP:EcoCyc.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
GO; GO:0016094; P:polyprenol biosynthetic process; IDA:EcoCyc.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
CDD; cd00475; Cis_IPPS; 1.
Gene3D; 3.40.1180.10; -; 1.
HAMAP; MF_01139; ISPT; 1.
InterPro; IPR001441; UPP_synth-like.
InterPro; IPR018520; UPP_synth-like_CS.
InterPro; IPR036424; UPP_synth-like_sf.
PANTHER; PTHR10291; PTHR10291; 1.
Pfam; PF01255; Prenyltransf; 1.
SUPFAM; SSF64005; SSF64005; 1.
TIGRFAMs; TIGR00055; uppS; 1.
PROSITE; PS01066; UPP_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Magnesium;
Metal-binding; Peptidoglycan synthesis; Reference proteome;
Transferase.
CHAIN 1 253 Ditrans,polycis-undecaprenyl-diphosphate
synthase ((2E,6E)-farnesyl-diphosphate
specific).
/FTId=PRO_0000123609.
REGION 26 30 Substrate binding.
REGION 71 73 Substrate binding. {ECO:0000250}.
REGION 200 202 Substrate binding.
ACT_SITE 26 26
ACT_SITE 74 74 Proton acceptor. {ECO:0000250}.
METAL 26 26 Magnesium.
METAL 199 199 Magnesium.
METAL 213 213 Magnesium.
BINDING 31 31 Substrate. {ECO:0000305|PubMed:15044730}.
BINDING 39 39 Substrate. {ECO:0000269|PubMed:15044730}.
BINDING 43 43 Substrate. {ECO:0000269|PubMed:15044730}.
BINDING 75 75 Substrate. {ECO:0000305|PubMed:15044730}.
BINDING 77 77 Substrate. {ECO:0000269|PubMed:15044730}.
BINDING 194 194 Substrate. {ECO:0000269|PubMed:15044730}.
BINDING 213 213 Isopentenyl diphosphate.
SITE 69 69 Required for continued chain elongation.
SITE 137 137 Important for determining product length.
MUTAGEN 26 26 D->A: Great decrease in activity.
{ECO:0000269|PubMed:11076526}.
MUTAGEN 31 31 W->F: Decrease in activity; reduced
affinity for decaprenyl diphosphate
substrate analog.
{ECO:0000269|PubMed:11744728}.
MUTAGEN 43 43 H->A: Great decreases in the catalytic
efficiency and the affinity for FPP and
IPP. {ECO:0000269|PubMed:12756244}.
MUTAGEN 62 62 I->A: Formation predominantly of C(60)
and C(65) polymers rather than the C(55)
polymer. {ECO:0000269|PubMed:11581264}.
MUTAGEN 69 69 A->L: Produces shorter polymers.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 71 71 S->A: Decrease in activity.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 73 73 E->A: Slight decrease in activity.
{ECO:0000269|PubMed:11076526,
ECO:0000269|PubMed:11581264}.
MUTAGEN 74 74 N->A: Decrease in activity.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 75 75 W->A,F: Decrease in activity; reduced
affinity for decaprenyl diphosphate
substrate analog.
{ECO:0000269|PubMed:11581264,
ECO:0000269|PubMed:11744728}.
MUTAGEN 77 77 R->A: Decrease in activity.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 81 81 E->A: Slight decrease in activity.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 91 91 W->F: Decrease in affinity for IPP.
{ECO:0000269|PubMed:11744728}.
MUTAGEN 103 103 H->A: No effect.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 105 105 V->A: Formation predominantly of C(60),
C(65) and C(70) polymers rather than the
C(55) polymer.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 137 137 L->A: Formation predominantly of a C(70)
polymer rather than the C(55) polymer.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 143 143 A->V: No effect on polymer length.
{ECO:0000269|PubMed:11581264}.
MUTAGEN 149 149 W->F: Decrease in affinity for IPP.
{ECO:0000269|PubMed:11744728}.
MUTAGEN 150 150 D->A: Great decrease in affinity for the
substrate. {ECO:0000269|PubMed:11076526}.
MUTAGEN 190 190 D->A: No effect.
{ECO:0000269|PubMed:11076526}.
MUTAGEN 198 198 E->A: No effect.
{ECO:0000269|PubMed:11076526}.
MUTAGEN 199 199 H->A: Great decreases in the catalytic
efficiency and in the affinity for IPP;
when associated with A-213.
{ECO:0000269|PubMed:12756244}.
MUTAGEN 207 207 W->F: Decrease in affinity for both IPP
and decaprenyl diphosphate substrate
analog. {ECO:0000269|PubMed:11744728}.
MUTAGEN 213 213 E->A: Great decrease in activity; reduced
affinity for IPP. Great decreases in the
catalytic efficiency and in the affinity
for IPP; when associated with A-199.
{ECO:0000269|PubMed:11076526,
ECO:0000269|PubMed:12756244}.
MUTAGEN 218 218 D->A: Slight decrease in activity.
{ECO:0000269|PubMed:11076526}.
MUTAGEN 221 221 W->F: Decrease in affinity for IPP.
{ECO:0000269|PubMed:11744728}.
MUTAGEN 223 223 D->A: No effect.
{ECO:0000269|PubMed:11076526}.
HELIX 15 17 {ECO:0000244|PDB:1X09}.
STRAND 19 25 {ECO:0000244|PDB:3SGV}.
HELIX 28 34 {ECO:0000244|PDB:3SGV}.
HELIX 39 59 {ECO:0000244|PDB:3SGV}.
STRAND 63 68 {ECO:0000244|PDB:3SGV}.
HELIX 72 75 {ECO:0000244|PDB:3SGV}.
HELIX 83 90 {ECO:0000244|PDB:3SGV}.
HELIX 93 102 {ECO:0000244|PDB:3SGV}.
STRAND 106 111 {ECO:0000244|PDB:3SGV}.
HELIX 113 115 {ECO:0000244|PDB:3SGV}.
HELIX 118 131 {ECO:0000244|PDB:3SGV}.
STRAND 138 144 {ECO:0000244|PDB:3SGV}.
HELIX 147 164 {ECO:0000244|PDB:3SGV}.
HELIX 169 171 {ECO:0000244|PDB:3SGV}.
HELIX 174 178 {ECO:0000244|PDB:3SGV}.
TURN 182 185 {ECO:0000244|PDB:3SGV}.
STRAND 191 197 {ECO:0000244|PDB:3SGV}.
STRAND 204 206 {ECO:0000244|PDB:3WYJ}.
HELIX 207 209 {ECO:0000244|PDB:3SGV}.
STRAND 213 216 {ECO:0000244|PDB:3SGV}.
HELIX 221 223 {ECO:0000244|PDB:3SGV}.
HELIX 226 239 {ECO:0000244|PDB:3SGV}.
SEQUENCE 253 AA; 28444 MW; 73DC9534C14CA7B9 CRC64;
MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV RRAVSFAANN
GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL HRHNVRLRII GDTSRFNSRL
QERIRKSEAL TAGNTGLTLN IAANYGGRWD IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH
VCMHELAPVD LVIRTGGEHR ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE
RRFGGTEPGD ETA


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EIAAB11423 All-trans-decaprenyl-diphosphate synthase subunit 2,C6orf210,Candidate tumor suppressor protein,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,DLP1,Homo sapiens,
E4915h Human Nuclear Undecaprenyl Pyrophosphate Synthase 96T
EIAAB11422 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Pdss2,Rat,Rattus norvegicus
NUTF2 NUS1 Gene nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae)
EIAAB11863 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,DPS1,Homo sapiens,Human,PDSS1,TPRT,TPT 1,Trans-prenyltransfera
201-20-2023 FDPS{farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase)}rabbit.pAb 0.2ml
CSB-EL008563RA Rat farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB27118 D10Ertd438e,Mouse,Mus musculus,NgBR,Ngbr,Nogo-B receptor,Nuclear undecaprenyl pyrophosphate synthase 1 homolog,Nus1
EIAAB27119 C6orf68,Homo sapiens,Human,NgBR,NGBR,Nogo-B receptor,Nuclear undecaprenyl pyrophosphate synthase 1 homolog,NUS1
CSB-EL016212MO Mouse nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae) (NUS1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL016212HU Human nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae) (NUS1) ELISA kit, Species Human, Sample Type serum, plasma 96T
26-323 GGPS1 is a member of the prenyltransferase family and has geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diph 0.05 mg
30-424 GGPS1 is a member of the prenyltransferase family with geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosp 0.05 mg
CSB-EL008563BO Bovine farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL008563CH Chicken farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL008563HU Human farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL008563MO Mouse farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA016212GA01HU Rabbit anti-human nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA016212GA01HU Rabbit anti-human nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA008563GA01HU Rabbit anti-human farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA008563GA01HU Rabbit anti-human farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
EIAAB11129 Dedol-PP synthase,Dehydrodolichyl diphosphate synthase,Dhdds,Mouse,Mus musculus
EIAAB11128 Dedol-PP synthase,Dehydrodolichyl diphosphate synthase,DHDDS,HDS,Homo sapiens,Human


 

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