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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation7 Publications

Catalytic activityi

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.UniRule annotation7 Publications

Enzyme regulationi

Competitively inhibited by glyphosate (PubMed:12430021, PubMed:6229418). Inhibited by (S)- and (R)-phosphonates analogs (PubMed:15736934). Inhibited by (R)-difluoromethyl analogs of the tetrahedral reaction intermediate (PubMed:16225867). Inhibited by bromopyruvate (PubMed:1899181).6 Publications

Kineticsi

  1. KM=0.0035 mM for S3P (at pH 7 and 25 degrees Celsius1 Publication
  2. KM=0.015 mM for PEP (at pH 7 and 25 degrees Celsius1 Publication
  3. KM=0.045 mM for PEP (at pH 7.5 and 25 degrees Celsius1 Publication
  4. KM=0.048 mM for S3P (at pH 7.5 and 25 degrees Celsius1 Publication
  5. KM=0.06 mM for PEP (at pH 7.5 and 25 degrees Celsius1 Publication
  6. KM=0.06 mM for S3P (at pH 7.5 and 25 degrees Celsius1 Publication
  7. KM=0.088 mM for PEP (at pH 6.8 and 20 degrees Celsius1 Publication
  8. KM=0.09 mM for S3P (at pH 5.5 and 20 degrees Celsius1 Publication
  9. KM=0.1 mM for PEP (at pH 5.5 and 20 degrees Celsius1 Publication
  10. KM=0.12 mM for S3P (at pH 6.8 and 20 degrees Celsius1 Publication
  1. Vmax=50 µmol/min/µg enzyme (at pH 7.5 and 25 degrees Celsius1 Publication
  2. Vmax=53 µmol/min/µg enzyme (at pH 5.5 and 20 degrees Celsius1 Publication
  3. Vmax=57 µmol/min/µg enzyme (at pH 7.5 and 25 degrees Celsius1 Publication

pH dependencei

Optimum pH is between 6 and 6.5.5 Publications

Pathway: chorismate biosynthesis

This protein is involved in step 6 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotationCurated
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG)
  2. 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD), 3-dehydroquinate dehydratase (aroD)
  4. Quinate/shikimate dehydrogenase (ydiB), Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK), Shikimate kinase 1 (aroK), Shikimate kinase 2 (aroL)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC), Chorismate synthase (aroC)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271Shikimate-3-phosphateUniRule annotation7 Publications
Binding sitei124 – 1241PhosphoenolpyruvateUniRule annotation4 Publications
Binding sitei197 – 1971Shikimate-3-phosphateUniRule annotation7 Publications
Active sitei313 – 3131Proton acceptorUniRule annotation7 Publications
Binding sitei336 – 3361Shikimate-3-phosphateUniRule annotation7 Publications
Binding sitei340 – 3401Shikimate-3-phosphateUniRule annotation8 Publications
Active sitei341 – 3411Proton donorUniRule annotation1 Publication1 Publication
Binding sitei344 – 3441PhosphoenolpyruvateUniRule annotation4 Publications
Binding sitei386 – 3861PhosphoenolpyruvateUniRule annotation4 Publications
Sitei408 – 4081Modified by bromopyruvate1 Publication
Binding sitei411 – 4111PhosphoenolpyruvateUniRule annotation4 Publications
Sitei411 – 4111Modified by bromopyruvate1 Publication

GO - Molecular functioni

  • 3-phosphoshikimate 1-carboxyvinyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:AROA-MONOMER.
ECOL316407:JW0891-MONOMER.
MetaCyc:AROA-MONOMER.
BRENDAi2.5.1.19. 2026.
SABIO-RKP0A6D3.
UniPathwayiUPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.19UniRule annotation6 Publications)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase1 PublicationUniRule annotation
Short name:
EPSP synthase1 PublicationUniRule annotation
Short name:
EPSPSUniRule annotationCurated
Gene namesi
Name:aroA1 PublicationUniRule annotation
Ordered Locus Names:b0908, JW0891
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10073. aroA.

Subcellular locationi

  • Cytoplasm UniRule annotationCurated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi96 – 961G → A: Insensitive to glyphosate with unaltered affinity for its first substrate S3P, but displays a 30-fold lower affinity for its second substrate PEP. 1 Publication
Mutagenesisi97 – 971T → I: This mutant is sensitive to glyphosate and causes a substantial decrease in the affinity for PEP. Insensitive to glyphosate but maintains high affinity for PEP. It causes a shift of residue G96 toward the glyphosate binding site, impairing efficient binding of glyphosate, while the side chain of I97 points away from the substrate binding site, facilitating PEP utilization; when associated with S-101. 1 Publication
Mutagenesisi101 – 1011P → A: Displays a slight decrease of the affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor. 2 Publications
Mutagenesisi101 – 1011P → G: Displays a slight decrease of the affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor. 2 Publications
Mutagenesisi101 – 1011P → L: Displays a 2-fold lower affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor. 2 Publications
Mutagenesisi101 – 1011P → S: Displays a slight decrease of the affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor. Insensitive to glyphosate but maintains high affinity for PEP. It causes a shift of residue G96 toward the glyphosate binding site, impairing efficient binding of glyphosate, while the side chain of I97 points away from the substrate binding site, facilitating PEP utilization; when associated with I-97. 2 Publications
Mutagenesisi313 – 3131D → A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4274273-phosphoshikimate 1-carboxyvinyltransferasePRO_0000088253Add
BLAST

Proteomic databases

PaxDbiP0A6D3.
PRIDEiP0A6D3.

2D gel databases

SWISS-2DPAGEP0A6D3.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-48256N.
IntActiP0A6D3. 3 interactions.
STRINGi511145.b0908.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi11 – 177Combined sources
Helixi22 – 3413Combined sources
Beta strandi35 – 439Combined sources
Helixi48 – 5912Combined sources
Beta strandi63 – 664Combined sources
Beta strandi68 – 703Combined sources
Beta strandi73 – 764Combined sources
Beta strandi79 – 813Combined sources
Beta strandi88 – 914Combined sources
Helixi96 – 10510Combined sources
Beta strandi108 – 1169Combined sources
Helixi119 – 1235Combined sources
Helixi127 – 1359Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi160 – 1689Combined sources
Helixi171 – 1799Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi187 – 1959Combined sources
Helixi199 – 21012Combined sources
Beta strandi216 – 2183Combined sources
Turni219 – 2213Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi235 – 2384Combined sources
Helixi243 – 25614Combined sources
Beta strandi257 – 2648Combined sources
Helixi272 – 2754Combined sources
Helixi276 – 2838Combined sources
Beta strandi286 – 2894Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi305 – 3073Combined sources
Turni312 – 3143Combined sources
Helixi315 – 3217Combined sources
Helixi322 – 3243Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi329 – 3335Combined sources
Helixi335 – 3395Combined sources
Beta strandi340 – 3423Combined sources
Helixi344 – 35411Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi363 – 3697Combined sources
Helixi385 – 3928Combined sources
Helixi393 – 3953Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi401 – 4055Combined sources
Helixi406 – 4116Combined sources
Helixi416 – 4238Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPSX-ray3.00A1-427[»]
1G6SX-ray1.50A1-427[»]
1G6TX-ray1.60A1-427[»]
1MI4X-ray1.70A1-427[»]
1P88NMR-A25-240[»]
1P89NMR-A25-240[»]
1Q0Imodel-A1-427[»]
1Q0Jmodel-A1-427[»]
1Q36X-ray1.60A1-427[»]
1X8RX-ray1.50A1-427[»]
1X8TX-ray1.90A1-427[»]
2AA9X-ray1.50A1-427[»]
2AAYX-ray1.55A1-427[»]
2PQ9X-ray1.60A1-427[»]
2QFQX-ray1.50A1-427[»]
2QFSX-ray1.55A1-427[»]
2QFTX-ray1.55A1-427[»]
2QFUX-ray1.60A1-427[»]
3FJXX-ray1.75A1-427[»]
3FJZX-ray1.70A1-427[»]
3FK0X-ray1.70A1-427[»]
3FK1X-ray1.70A1-427[»]
ProteinModelPortaliP0A6D3.
SMRiP0A6D3. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6D3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 232Shikimate-3-phosphate bindingUniRule annotation8 Publications
Regioni94 – 974PhosphoenolpyruvateUniRule annotation4 Publications
Regioni169 – 1713Shikimate-3-phosphate bindingUniRule annotation8 Publications

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiCOG0128.
HOGENOMiHOG000247372.
InParanoidiP0A6D3.
KOiK00800.
OMAiGADIEWG.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP0A6D3.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF000505. EPSPS. 1 hit.
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
PROSITEiPS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV
60 70 80 90 100
RHMLNALTAL GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR
110 120 130 140 150
PLAAALCLGS NDIVLTGEPR MKERPIGHLV DALRLGGAKI TYLEQENYPP
160 170 180 190 200
LRLQGGFTGG NVDVDGSVSS QFLTALLMTA PLAPEDTVIR IKGDLVSKPY
210 220 230 240 250
IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE GDASSASYFL
260 270 280 290 300
AAAAIKGGTV KVTGIGRNSM QGDIRFADVL EKMGATICWG DDYISCTRGE
310 320 330 340 350
LNAIDMDMNH IPDAAMTIAT AALFAKGTTT LRNIYNWRVK ETDRLFAMAT
360 370 380 390 400
ELRKVGAEVE EGHDYIRITP PEKLNFAEIA TYNDHRMAMC FSLVALSDTP
410 420
VTILDPKCTA KTFPDYFEQL ARISQAA
Length:427
Mass (Da):46,096
Last modified:June 7, 2005 - v1
Checksum:iB1F55469EB4D9F97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231S → T in CAA25223 (Ref. 1) Curated
Sequence conflicti330 – 3301T → R in CAA25223 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00557 Genomic DNA. Translation: CAA25223.1.
U00096 Genomic DNA. Translation: AAC73994.1.
AP009048 Genomic DNA. Translation: BAA35643.1.
U31523 Genomic DNA. Translation: AAA81514.1.
PIRiC64830. XUECVS.
RefSeqiNP_415428.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.
GeneIDi945528.
KEGGiecj:Y75_p0880.
eco:b0908.
PATRICi32117029. VBIEscCol129921_0939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00557 Genomic DNA. Translation: CAA25223.1.
U00096 Genomic DNA. Translation: AAC73994.1.
AP009048 Genomic DNA. Translation: BAA35643.1.
U31523 Genomic DNA. Translation: AAA81514.1.
PIRiC64830. XUECVS.
RefSeqiNP_415428.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPSX-ray3.00A1-427[»]
1G6SX-ray1.50A1-427[»]
1G6TX-ray1.60A1-427[»]
1MI4X-ray1.70A1-427[»]
1P88NMR-A25-240[»]
1P89NMR-A25-240[»]
1Q0Imodel-A1-427[»]
1Q0Jmodel-A1-427[»]
1Q36X-ray1.60A1-427[»]
1X8RX-ray1.50A1-427[»]
1X8TX-ray1.90A1-427[»]
2AA9X-ray1.50A1-427[»]
2AAYX-ray1.55A1-427[»]
2PQ9X-ray1.60A1-427[»]
2QFQX-ray1.50A1-427[»]
2QFSX-ray1.55A1-427[»]
2QFTX-ray1.55A1-427[»]
2QFUX-ray1.60A1-427[»]
3FJXX-ray1.75A1-427[»]
3FJZX-ray1.70A1-427[»]
3FK0X-ray1.70A1-427[»]
3FK1X-ray1.70A1-427[»]
ProteinModelPortaliP0A6D3.
SMRiP0A6D3. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48256N.
IntActiP0A6D3. 3 interactions.
STRINGi511145.b0908.

Chemistry

BindingDBiP0A6D3.
ChEMBLiCHEMBL5033.

2D gel databases

SWISS-2DPAGEP0A6D3.

Proteomic databases

PaxDbiP0A6D3.
PRIDEiP0A6D3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.
GeneIDi945528.
KEGGiecj:Y75_p0880.
eco:b0908.
PATRICi32117029. VBIEscCol129921_0939.

Organism-specific databases

EchoBASEiEB0071.
EcoGeneiEG10073. aroA.

Phylogenomic databases

eggNOGiCOG0128.
HOGENOMiHOG000247372.
InParanoidiP0A6D3.
KOiK00800.
OMAiGADIEWG.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP0A6D3.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00089.
BioCyciEcoCyc:AROA-MONOMER.
ECOL316407:JW0891-MONOMER.
MetaCyc:AROA-MONOMER.
BRENDAi2.5.1.19. 2026.
SABIO-RKP0A6D3.

Miscellaneous databases

EvolutionaryTraceiP0A6D3.
PROiP0A6D3.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth.
InterProiIPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PfamiPF00275. EPSP_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF000505. EPSPS. 1 hit.
SUPFAMiSSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
PROSITEiPS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete amino acid sequence of Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase."
    Duncan K., Lewendon A., Coggins J.R.
    FEBS Lett. 170:59-63(1984)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-427.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain of Escherichia coli."
    Duncan K., Lewendon A., Coggins J.R.
    FEBS Lett. 165:121-127(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
  7. "5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli --the substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-408 and Lys-411."
    Huynh Q.K.
    Arch. Biochem. Biophys. 284:407-412(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  8. "Photo-oxidation of 5-enolpyruvoylshikimate-3-phosphate synthase from Escherichia coli: evidence for a reactive imidazole group (His385) at the herbicide glyphosate-binding site."
    Huynh Q.K.
    Biochem. J. 290:525-530(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOTO-OXIDATION AT HIS-385.
  9. "Structure and topological symmetry of the glyphosate target 5-enol-pyruvylshikimate-3-phosphate synthase: a distinctive protein fold."
    Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.-S., Dayringer H.E., Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A., Padgette S.R., Kishore G.M.
    Proc. Natl. Acad. Sci. U.S.A. 88:5046-5050(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  10. "Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail."
    Schonbrunn E., Eschenburg S., Shuttleworth W.A., Schloss J.V., Amrhein N., Evans J.N., Kabsch W.
    Proc. Natl. Acad. Sci. U.S.A. 98:1376-1380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOG.
  11. "How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli."
    Eschenburg S., Healy M.L., Priestman M.A., Lushington G.H., Schonbrunn E.
    Planta 216:129-135(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-96 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-96, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  12. "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."
    Eschenburg S., Kabsch W., Healy M.L., Schonbrunn E.
    J. Biol. Chem. 278:49215-49222(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANT ALA-313 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-313, ACTIVE SITE, REACTION MECHANISM.
  13. "Letter: Substrate-induced structural changes to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase."
    Young J.K., Stauffer M.E., Kim H.J., Helms G.L., Evans J.N.S.
    Submitted (MAY-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 25-240.
  14. "Interaction of phosphonate analogues of the tetrahedral reaction intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic detail."
    Priestman M.A., Healy M.L., Becker A., Alberg D.G., Bartlett P.A., Lushington G.H., Schonbrunn E.
    Biochemistry 44:3241-3248(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOGS, ENZYME REGULATION, ACTIVE SITE, REACTION MECHANISM.
  15. "Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate."
    Priestman M.A., Healy M.L., Funke T., Becker A., Schonbrunn E.
    FEBS Lett. 579:5773-5780(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  16. "Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-phosphate synthases by tetrahedral reaction intermediate analogues."
    Funke T., Healy-Fried M.L., Han H., Alberg D.G., Bartlett P.A., Schonbrunn E.
    Biochemistry 46:13344-13351(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOGS, FUNCTION, ACTIVE SITE, ENZYME REGULATION.
  17. "Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase."
    Healy-Fried M.L., Funke T., Priestman M.A., Han H., Schonbrunn E.
    J. Biol. Chem. 282:32949-32955(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS L101 AND S101 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PRO-101, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.
  18. "Structural basis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli."
    Funke T., Yang Y., Han H., Healy-Fried M., Olesen S., Becker A., Schonbrunn E.
    J. Biol. Chem. 284:9854-9860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-97 AND PRO-101, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiAROA_ECOLI
AccessioniPrimary (citable) accession number: P0A6D3
Secondary accession number(s): P07638, P78222
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: June 24, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.