(2Z,6E)-farnesyl diphosphate synthase

Details

Name
(2Z,6E)-farnesyl diphosphate synthase
Synonyms
  • 2.5.1.68
  • Short-chain Z-isoprenyl diphosphate synthase
  • Z-FPP synthase
  • Z-FPPS
  • Z-isoprenyl diphosphate synthase
  • Z-Polyprenyl diphosphate synthase
Gene Name
Not Available
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051237|(2Z,6E)-farnesyl diphosphate synthase
MEIIPPRLKEPLYRLYELRLRQGLAASKSDLPRHIAVLCDGNRRWARSAGYDDVSYGYRM
GAAKIAEMLRWCHEAGIELATVYLLSTENLQRDPDELAALIEIITDVVEEICAPANHWSV
RTVGDLGLIGEEPARRLRGAVESTPEVASFHVNVAVGYGGRREIVDAVRALLSKELANGA
TAEELVDAVTVEGISENLYTSGQPDPDLVIRTSGEQRLSGFLLWQSAYSEMWFTEAHWPA
FRHVDFLRALRDYSARHRSYGR
Number of residues
262
Molecular Weight
29409.955
Theoretical pI
Not Available
GO Classification
Functions
magnesium ion binding / manganese ion binding / polyprenyltransferase activity / Z-farnesyl diphosphate synthase activity
Processes
polyprenol biosynthetic process
Components
cytosol / plasma membrane
General Function
Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall.
Specific Function
Magnesium ion binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051238|(2Z,6E)-farnesyl diphosphate synthase
GTGGAGATCATCCCGCCGCGGCTCAAAGAGCCGTTGTACCGGCTCTACGAGCTGCGCCTG
CGGCAGGGCTTGGCCGCCTCGAAATCCGACCTGCCCCGGCACATAGCCGTGCTGTGCGAC
GGCAACCGGCGATGGGCGCGCAGCGCGGGCTACGACGACGTCAGCTACGGCTACCGGATG
GGTGCGGCCAAGATCGCCGAAATGCTGCGGTGGTGCCACGAAGCCGGCATCGAACTGGCC
ACCGTCTATCTGCTGTCCACCGAAAACCTGCAGCGCGATCCCGACGAGCTTGCAGCACTC
ATCGAGATCATCACCGATGTCGTGGAAGAGATCTGCGCACCGGCCAACCACTGGAGTGTG
CGGACGGTCGGGGATCTGGGGTTGATCGGCGAGGAACCGGCCCGGCGGCTGCGCGGTGCG
GTGGAATCCACCCCGGAGGTGGCCTCGTTTCATGTCAACGTTGCTGTTGGCTACGGCGGG
CGCCGCGAGATCGTCGACGCTGTGCGCGCGTTGTTGAGCAAGGAACTCGCCAACGGGGCC
ACCGCGGAGGAACTCGTCGACGCGGTGACCGTCGAGGGTATCTCGGAAAACCTGTACACC
TCAGGCCAACCCGACCCCGATTTGGTGATACGCACCTCCGGCGAGCAACGCTTGTCCGGG
TTCTTGCTGTGGCAAAGCGCCTACTCGGAGATGTGGTTCACCGAGGCGCACTGGCCGGCG
TTTCGCCACGTCGATTTTCTACGCGCGCTGCGTGACTACAGTGCGAGGCATCGCAGCTAC
GGCAGGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WFF5
UniProtKB Entry NameZFPP_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Crick DC, Schulbach MC, Zink EE, Macchia M, Barontini S, Besra GS, Brennan PJ: Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis. J Bacteriol. 2000 Oct;182(20):5771-8. [Article]
  3. Schulbach MC, Brennan PJ, Crick DC: Identification of a short (C15) chain Z-isoprenyl diphosphate synthase and a homologous long (C50) chain isoprenyl diphosphate synthase in Mycobacterium tuberculosis. J Biol Chem. 2000 Jul 28;275(30):22876-81. [Article]
  4. Schulbach MC, Mahapatra S, Macchia M, Barontini S, Papi C, Minutolo F, Bertini S, Brennan PJ, Crick DC: Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J Biol Chem. 2001 Apr 13;276(15):11624-30. Epub 2001 Jan 4. [Article]
  5. Noike M, Ambo T, Kikuchi S, Suzuki T, Yamashita S, Takahashi S, Kurokawa H, Mahapatra S, Crick DC, Koyama T: Product chain-length determination mechanism of Z,E-farnesyl diphosphate synthase. Biochem Biophys Res Commun. 2008 Dec 5;377(1):17-22. doi: 10.1016/j.bbrc.2008.09.014. Epub 2008 Sep 13. [Article]
  6. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  7. Wang W, Dong C, McNeil M, Kaur D, Mahapatra S, Crick DC, Naismith JH: The structural basis of chain length control in Rv1086. J Mol Biol. 2008 Aug 1;381(1):129-40. doi: 10.1016/j.jmb.2008.05.060. Epub 2008 Jul 1. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07780Farnesyl diphosphateexperimentalunknownDetails
DB02552Geranyl DiphosphateexperimentalunknownDetails