Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei33Shikimate-3-phosphateUniRule annotation2 Publications1
Binding sitei128PhosphoenolpyruvateUniRule annotation1 Publication1
Active sitei326Proton acceptorUniRule annotation1 Publication1
Binding sitei353Shikimate-3-phosphateUniRule annotation2 Publications1
Active sitei354Proton donorUniRule annotation1 Publication1
Binding sitei357PhosphoenolpyruvateUniRule annotation1 Publication1
Binding sitei405PhosphoenolpyruvateUniRule annotation1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi100A → G: Confers resistance to glyphosate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000882151 – 4553-phosphoshikimate 1-carboxyvinyltransferaseAdd BLAST455

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

Secondary structure

1455
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Beta strandi19 – 23Combined sources5
Helixi28 – 40Combined sources13
Beta strandi41 – 49Combined sources9
Helixi54 – 65Combined sources12
Beta strandi69 – 73Combined sources5
Beta strandi76 – 82Combined sources7
Helixi100 – 111Combined sources12
Beta strandi113 – 120Combined sources8
Helixi125 – 127Combined sources3
Helixi131 – 139Combined sources9
Beta strandi143 – 147Combined sources5
Turni148 – 150Combined sources3
Beta strandi151 – 157Combined sources7
Beta strandi166 – 168Combined sources3
Beta strandi170 – 172Combined sources3
Helixi174 – 185Combined sources12
Beta strandi187 – 197Combined sources11
Helixi202 – 209Combined sources8
Beta strandi214 – 218Combined sources5
Beta strandi224 – 229Combined sources6
Beta strandi238 – 240Combined sources3
Helixi245 – 257Combined sources13
Beta strandi262 – 269Combined sources8
Helixi272 – 274Combined sources3
Helixi276 – 284Combined sources9
Beta strandi287 – 296Combined sources10
Beta strandi299 – 307Combined sources9
Helixi318 – 323Combined sources6
Helixi325 – 327Combined sources3
Helixi328 – 335Combined sources8
Beta strandi338 – 344Combined sources7
Helixi348 – 352Combined sources5
Beta strandi353 – 355Combined sources3
Helixi357 – 367Combined sources11
Beta strandi371 – 374Combined sources4
Beta strandi379 – 382Combined sources4
Helixi404 – 414Combined sources11
Beta strandi417 – 419Combined sources3
Beta strandi421 – 424Combined sources4
Helixi429 – 431Combined sources3
Helixi436 – 443Combined sources8
Beta strandi446 – 449Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R4E4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni28 – 29Shikimate-3-phosphate bindingUniRule annotation2 Publications2
Regioni98 – 101PhosphoenolpyruvateUniRule annotation1 Publication4

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotationCurated

Family and domain databases

CDDicd01556. EPSP_synthase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti2S → L AA sequence (PubMed:8598558).Curated1

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

CDDicd01556. EPSP_synthase. 1 hit.
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: November 30, 2016
This is version 89 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.