3-phosphoshikimate 1-carboxyvinyltransferase

Details

Name
3-phosphoshikimate 1-carboxyvinyltransferase
Synonyms
  • 2.5.1.19
  • 5-enolpyruvylshikimate-3-phosphate synthase
  • EPSP synthase
  • EPSPS
Gene Name
aroA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016408|3-phosphoshikimate 1-carboxyvinyltransferase
MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTAL
GVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPR
MKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTA
PLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVE
GDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGE
LNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVE
EGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQL
ARISQAA
Number of residues
427
Molecular Weight
46095.29
Theoretical pI
5.27
GO Classification
Functions
3-phosphoshikimate 1-carboxyvinyltransferase activity
Processes
aromatic amino acid family biosynthetic process / chorismate biosynthetic process
Components
cytosol
General Function
3-phosphoshikimate 1-carboxyvinyltransferase activity
Specific Function
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016409|3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
ATGGAATCCCTGACGTTACAACCCATCGCTCGTGTCGATGGCACTATTAATCTGCCCGGT
TCCAAGAGCGTTTCTAACCGCGCTTTATTGCTGGCGGCATTAGCACACGGCAAAACAGTA
TTAACCAATCTGCTGGATAGCGATGACGTGCGCCATATGCTGAATGCATTAACAGCGTTA
GGGGTAAGCTATACGCTTTCAGCCGATCGTACGCGTTGCGAAATTATCGGTAACGGCGGT
CCATTACACGCAGAAGGTGCCCTGGAGTTGTTCCTCGGTAACGCCGGAACGGCAATGCGT
CCGCTGGCGGCAGCTCTTTGTCTGGGTAGCAATGATATTGTGCTGACCGGTGAGCCGCGT
ATGAAAGAACGCCCGATTGGTCATCTGGTGGATGCGCTGCGCCTGGGCGGGGCGAAGATC
ACTTACCTGGAACAAGAAAATTATCCGCCGTTGCGTTTACAGGGCGGCTTTACTGGCGGC
AACGTTGACGTTGATGGCTCCGTTTCCAGCCAATTCCTCACCGCACTGTTAATGACTGCG
CCTCTTGCGCCGGAAGATACGGTGATTCGTATTAAAGGCGATCTGGTTTCTAAACCTTAT
ATCGACATCACACTCAATCTGATGAAGACGTTTGGTGTTGAAATTGAAAATCAGCACTAT
CAACAATTTGTCGTAAAAGGCGGGCAGTCTTATCAGTCTCCGGGTACTTATTTGGTCGAA
GGCGATGCATCTTCGGCTTCTTACTTTCTGGCAGCAGCAGCAATCAAAGGCGGCACTGTA
AAAGTGACCGGTATTGGACGTAACAGTATGCAGGGTGATATTCGCTTTGCTGATGTGCTG
GAAAAAATGGGCGCGACCATTTGCTGGGGCGATGATTATATTTCCTGCACGCGTGGTGAA
CTGAACGCTATTGATATGGATATGAACCATATTCCTGATGCGGCGATGACCATTGCCACG
GCGGCGTTATTTGCAAAAGGCACCACCACGCTGCGCAATATCTATAACTGGCGTGTTAAA
GAGACCGATCGCCTGTTTGCGATGGCAACAGAACTGCGTAAAGTCGGCGCGGAAGTGGAA
GAGGGGCACGATTACATTCGTATCACTCCTCCGGAAAAACTGAACTTTGCCGAGATCGCG
ACATACAATGATCACCGGATGGCGATGTGTTTCTCGCTGGTGGCGTTGTCAGATACACCA
GTGACGATTCTTGATCCCAAATGCACGGCCAAAACATTTCCGGATTATTTCGAGCAGCTG
GCGCGGATTAGCCAGGCAGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A6D3
UniProtKB Entry NameAROA_ECOLI
GenBank Protein ID40966
GenBank Gene IDX00557
General References
  1. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [PubMed:8905232]
  2. 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]
  3. 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]
  4. Duncan K, Lewendon A, Coggins JR: The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain of Escherichia coli. FEBS Lett. 1984 Jan 2;165(1):121-7. [PubMed:6229418]
  5. Huynh QK: 5-Enolpyruvylshikimate-3-phosphate synthase from Escherichia coli--the substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-408 and Lys-411. Arch Biochem Biophys. 1991 Feb 1;284(2):407-12. [PubMed:1899181]
  6. Huynh QK: Photo-oxidation of 5-enolpyruvoylshikimate-3-phosphate synthase from Escherichia coli: evidence for a reactive imidazole group (His385) at the herbicide glyphosate-binding site. Biochem J. 1993 Mar 1;290 ( Pt 2):525-30. [PubMed:8452542]
  7. Stallings WC, Abdel-Meguid SS, Lim LW, Shieh HS, Dayringer HE, Leimgruber NK, Stegeman RA, Anderson KS, Sikorski JA, Padgette SR, Kishore GM: Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):5046-50. [PubMed:11607190]
  8. Schonbrunn E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W: Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1376-80. [PubMed:11171958]
  9. Eschenburg S, Healy ML, Priestman MA, Lushington GH, Schonbrunn E: How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli. Planta. 2002 Nov;216(1):129-35. Epub 2002 Nov 12. [PubMed:12430021]
  10. Eschenburg S, Kabsch W, Healy ML, Schonbrunn E: A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states. J Biol Chem. 2003 Dec 5;278(49):49215-22. Epub 2003 Sep 16. [PubMed:13129913]
  11. Priestman MA, Healy ML, Becker A, Alberg DG, Bartlett PA, Lushington GH, Schonbrunn E: Interaction of phosphonate analogues of the tetrahedral reaction intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic detail. Biochemistry. 2005 Mar 8;44(9):3241-8. [PubMed:15736934]
  12. Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E: Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct 24;579(25):5773-80. [PubMed:16225867]
  13. Funke T, Healy-Fried ML, Han H, Alberg DG, Bartlett PA, Schonbrunn E: Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-phosphate synthases by tetrahedral reaction intermediate analogues. Biochemistry. 2007 Nov 20;46(46):13344-51. Epub 2007 Oct 25. [PubMed:17958399]
  14. Healy-Fried ML, Funke T, Priestman MA, Han H, Schonbrunn E: Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase. J Biol Chem. 2007 Nov 9;282(45):32949-55. Epub 2007 Sep 12. [PubMed:17855366]
  15. Funke T, Yang Y, Han H, Healy-Fried M, Olesen S, Becker A, Schonbrunn E: Structural basis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli. J Biol Chem. 2009 Apr 10;284(15):9854-60. doi: 10.1074/jbc.M809771200. Epub 2009 Feb 11. [PubMed:19211556]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01942Formic acidexperimental, investigationalunknownDetails
DB031165-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-PhosphateexperimentalunknownDetails
DB04328Shikimate-3-PhosphateexperimentalunknownDetails
DB04539GlyphosateexperimentalunknownDetails