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Sequence of UPPS_ECOLI

EC Number:2.5.1.31

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
P60472
Escherichia coli (strain K12)
253
28444
Reaction
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
Other sequences found for EC No. 2.5.1.31

General information:

Sequence
show sequence in fasta format
  0 MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV RRAVSFAANN
 60 GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL HRHNVRLRII GDTSRFNSRL
120 QERIRKSEAL TAGNTGLTLN IAANYGGRWD IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH
180 VCMHELAPVD LVIRTGGEHR ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE
240 RRFGGTEPGD ETA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
247653
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
247654
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
0-0
2006
247655
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
247656
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
247657
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
247658
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
247659
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
247660
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
247661
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
247662
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
247663
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
247664
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
247665
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