Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)

Details

Name
Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)
Synonyms
  • 2.5.1.31
  • Ditrans,polycis-undecaprenylcistransferase
  • rth
  • UDS
  • Undecaprenyl diphosphate synthase
  • Undecaprenyl pyrophosphate synthase
  • UPP synthase
  • uppS
  • yaeS
Gene Name
ispU
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0006536|Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)
MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANN
GIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRL
QERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQH
VCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRE
RRFGGTEPGDETA
Number of residues
253
Molecular Weight
28443.92
Theoretical pI
6.96
GO Classification
Functions
di-trans,poly-cis-decaprenylcistransferase activity / magnesium ion binding
Processes
cell cycle / cell division / cell wall organization / Gram-negative-bacterium-type cell wall biogenesis / peptidoglycan biosynthetic process / polyprenol biosynthetic process / regulation of cell shape
Components
cytoplasm / cytosol
General Function
Magnesium ion binding
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012345|Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (ispU)
GTGATGTTGTCTGCTACTCAACCACTTAGCGAAAAATTGCCAGCGCATGGCTGCCGTCAT
GTTGCGATCATTATGGACGGCAATGGCCGCTGGGCAAAAAAGCAAGGGAAGATTCGTGCC
TTTGGGCATAAAGCCGGGGCAAAATCCGTCCGCCGGGCTGTCTCTTTTGCGGCCAACAAC
GGTATTGAGGCGTTAACGCTGTATGCCTTTAGTAGTGAAAACTGGAACCGACCAGCGCAG
GAAGTCAGTGCGTTAATGGAACTGTTTGTGTGGGCGCTCGATAGCGAAGTAAAAAGTCTG
CACCGACATAACGTGCGTCTGCGTATTATTGGCGATACCAGTCGCTTTAACTCGCGTTTG
CAAGAACGTATTCGTAAATCTGAAGCGCTAACAGCCGGGAATACCGGTCTGACGCTGAAT
ATTGCGGCGAACTACGGTGGACGTTGGGATATAGTCCAGGGAGTCAGGCAACTGGCTGAA
AAGGTGCAGCAAGGAAACCTGCAACCAGATCAGATAGATGAAGAGATGCTAAACCAGCAT
GTCTGTATGCATGAACTGGCCCCTGTAGATTTAGTAATTAGGACTGGGGGGGAGCATCGC
ATTAGTAACTTTTTGCTTTGGCAAATTGCCTATGCCGAACTTTACTTTACAGATGTTCTC
TGGCCCGATTTCGATGAACAAGACTTTGAAGGGGCGTTAAATGCCTTTGCTAATCGAGAG
CGTCGTTTCGGCGGCACCGAGCCCGGTGATGAAACAGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP60472
UniProtKB Entry NameUPPS_ECOLI
GenBank Gene IDU00096
General References
  1. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [PubMed:9278503]
  2. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed:16738553]
  3. Apfel CM, 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. 1999 Jan;181(2):483-92. [PubMed:9882662]
  4. 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. 1999 May;181(9):2733-8. [PubMed:10217761]
  5. Pan JJ, Yang LW, Liang PH: Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis. Biochemistry. 2000 Nov 14;39(45):13856-61. [PubMed:11076526]
  6. Chen YH, Chen AP, Chen CT, Wang AH, Liang PH: Probing the conformational change of Escherichia coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutants. J Biol Chem. 2002 Mar 1;277(9):7369-76. Epub 2001 Dec 14. [PubMed:11744728]
  7. Lu YP, Liu HG, Teng KH, Liang PH: Mechanism of cis-prenyltransferase reaction probed by substrate analogues. Biochem Biophys Res Commun. 2010 Oct 1;400(4):758-62. doi: 10.1016/j.bbrc.2010.09.001. Epub 2010 Sep 7. [PubMed:20828539]
  8. Ko TP, Chen YK, Robinson H, Tsai PC, Gao YG, Chen AP, Wang AH, Liang PH: Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J Biol Chem. 2001 Dec 14;276(50):47474-82. Epub 2001 Oct 1. [PubMed:11581264]
  9. Chang SY, Ko TP, Liang PH, Wang AH: Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton. J Biol Chem. 2003 Aug 1;278(31):29298-307. Epub 2003 May 19. [PubMed:12756244]
  10. Chang SY, Ko TP, Chen AP, Wang AH, Liang PH: Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies. Protein Sci. 2004 Apr;13(4):971-8. [PubMed:15044730]
  11. Guo RT, Ko TP, Chen AP, Kuo CJ, Wang AH, Liang PH: 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. 2005 May 27;280(21):20762-74. Epub 2005 Mar 23. [PubMed:15788389]
  12. Guo RT, Cao R, Liang PH, Ko TP, Chang TH, Hudock MP, Jeng WY, Chen CK, Zhang Y, Song Y, Kuo CJ, Yin F, Oldfield E, Wang AH: Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases. Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10022-7. Epub 2007 May 29. [PubMed:17535895]
  13. Sinko W, de Oliveira C, Williams S, Van Wynsberghe A, Durrant JD, Cao R, Oldfield E, McCammon JA: Applying molecular dynamics simulations to identify rarely sampled ligand-bound conformational states of undecaprenyl pyrophosphate synthase, an antibacterial target. Chem Biol Drug Des. 2011 Jun;77(6):412-20. doi: 10.1111/j.1747-0285.2011.01101.x. Epub 2011 Mar 29. [PubMed:21294851]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04695Farnesyl thiopyrophosphateexperimentalunknownDetails
DB04714ISOPENTENYL PYROPHOSPHATEexperimentalunknownDetails
DB07404(1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDexperimentalunknownDetails
DB07409(1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDexperimentalunknownDetails
DB07410[2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACIDexperimentalunknownDetails
DB07426[1-HYDROXY-2-(1,1':3',1''-TERPHENYL-3-YLOXY)ETHANE-1,1-DIYL]BIS(PHOSPHONIC ACID)experimentalunknownDetails
DB07780Farnesyl diphosphateexperimentalunknownDetails