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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Agrobacterium sp. (strain CP4)
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 annotation2 Publications

Catalytic activityi

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

Enzyme regulationi

Competitively inhibited by glyphosate, (R)-difluoromethyl and (R)-phosphonate analogs of the tetrahedral reaction intermediate.1 Publication

Pathwayi: 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. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. no protein annotated in this organism
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 sitei33 – 331Shikimate-3-phosphateUniRule annotation2 Publications
Binding sitei128 – 1281PhosphoenolpyruvateUniRule annotation1 Publication
Active sitei326 – 3261Proton acceptorUniRule annotation1 Publication
Binding sitei353 – 3531Shikimate-3-phosphateUniRule annotation2 Publications
Active sitei354 – 3541Proton donorUniRule annotation1 Publication
Binding sitei357 – 3571PhosphoenolpyruvateUniRule annotation1 Publication
Binding sitei405 – 4051PhosphoenolpyruvateUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Herbicide resistance

Enzyme and pathway databases

BRENDAi2.5.1.19. 206.
UniPathwayiUPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.19UniRule annotation)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase1 PublicationUniRule annotation
Short name:
EPSP synthaseUniRule annotation
Short name:
EPSPSUniRule annotation
Gene namesi
Name:aroAUniRule annotation
OrganismiAgrobacterium sp. (strain CP4)
Taxonomic identifieri268951 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Introduced by genetic manipulation and expressed in glyphosate-tolerant soybean, canola, cotton and maize by Monsanto. Developed to provide new weed-control options for farmers. Expression of this protein in plants imparts high levels of glyphosate tolerance.Curated

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001A → G: Confers resistance to glyphosate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4554553-phosphoshikimate 1-carboxyvinyltransferasePRO_0000088215Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi19 – 235Combined sources
Helixi28 – 4013Combined sources
Beta strandi41 – 499Combined sources
Helixi54 – 6512Combined sources
Beta strandi69 – 735Combined sources
Beta strandi76 – 827Combined sources
Helixi100 – 11112Combined sources
Beta strandi113 – 1208Combined sources
Helixi125 – 1273Combined sources
Helixi131 – 1399Combined sources
Beta strandi143 – 1475Combined sources
Turni148 – 1503Combined sources
Beta strandi151 – 1577Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1723Combined sources
Helixi174 – 18512Combined sources
Beta strandi187 – 19711Combined sources
Helixi202 – 2098Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi238 – 2403Combined sources
Helixi245 – 25713Combined sources
Beta strandi262 – 2698Combined sources
Helixi272 – 2743Combined sources
Helixi276 – 2849Combined sources
Beta strandi287 – 29610Combined sources
Beta strandi299 – 3079Combined sources
Helixi318 – 3236Combined sources
Helixi325 – 3273Combined sources
Helixi328 – 3358Combined sources
Beta strandi338 – 3447Combined sources
Helixi348 – 3525Combined sources
Beta strandi353 – 3553Combined sources
Helixi357 – 36711Combined sources
Beta strandi371 – 3744Combined sources
Beta strandi379 – 3824Combined sources
Helixi404 – 41411Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi421 – 4244Combined sources
Helixi429 – 4313Combined sources
Helixi436 – 4438Combined sources
Beta strandi446 – 4494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GG4X-ray2.10A1-455[»]
2GG6X-ray1.64A1-455[»]
2GGAX-ray1.70A1-455[»]
2GGDX-ray1.70A1-455[»]
2PQBX-ray1.80A6-450[»]
2PQCX-ray1.60A6-450[»]
2PQDX-ray1.77A6-450[»]
ProteinModelPortaliQ9R4E4.
SMRiQ9R4E4. Positions 6-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R4E4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 292Shikimate-3-phosphate bindingUniRule annotation2 Publications
Regioni98 – 1014PhosphoenolpyruvateUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotationCurated

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth. 1 hit.
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.

Q9R4E4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHGASSRPA TARKSSGLSG TVRIPGDKSI SHRSFMFGGL ASGETRITGL
60 70 80 90 100
LEGEDVINTG KAMQAMGARI RKEGDTWIID GVGNGGLLAP EAPLDFGNAA
110 120 130 140 150
TGCRLTMGLV GVYDFDSTFI GDASLTKRPM GRVLNPLREM GVQVKSEDGD
160 170 180 190 200
RLPVTLRGPK TPTPITYRVP MASAQVKSAV LLAGLNTPGI TTVIEPIMTR
210 220 230 240 250
DHTEKMLQGF GANLTVETDA DGVRTIRLEG RGKLTGQVID VPGDPSSTAF
260 270 280 290 300
PLVAALLVPG SDVTILNVLM NPTRTGLILT LQEMGADIEV INPRLAGGED
310 320 330 340 350
VADLRVRSST LKGVTVPEDR APSMIDEYPI LAVAAAFAEG ATVMNGLEEL
360 370 380 390 400
RVKESDRLSA VANGLKLNGV DCDEGETSLV VRGRPDGKGL GNASGAAVAT
410 420 430 440 450
HLDHRIAMSF LVMGLVSENP VTVDDATMIA TSFPEFMDLM AGLGAKIELS

DTKAA
Length:455
Mass (Da):47,588
Last modified:May 30, 2000 - v2
Checksum:i236580D08D6EF422
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → L AA sequence (PubMed:8598558).Curated

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GG4X-ray2.10A1-455[»]
2GG6X-ray1.64A1-455[»]
2GGAX-ray1.70A1-455[»]
2GGDX-ray1.70A1-455[»]
2PQBX-ray1.80A6-450[»]
2PQCX-ray1.60A6-450[»]
2PQDX-ray1.77A6-450[»]
ProteinModelPortaliQ9R4E4.
SMRiQ9R4E4. Positions 6-450.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00053; UER00089.
BRENDAi2.5.1.19. 206.

Miscellaneous databases

EvolutionaryTraceiQ9R4E4.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth. 1 hit.
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...

Entry informationi

Entry nameiAROA_AGRSC
AccessioniPrimary (citable) accession number: Q9R4E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 14, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Genetically modified food

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.