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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

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. Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. 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)DescriptionActionsGraphical viewLength
Binding sitei27Shikimate-3-phosphateUniRule annotation7 Publications1
Binding sitei124PhosphoenolpyruvateUniRule annotation4 Publications1
Binding sitei197Shikimate-3-phosphateUniRule annotation7 Publications1
Active sitei313Proton acceptorUniRule annotation7 Publications1
Binding sitei336Shikimate-3-phosphateUniRule annotation7 Publications1
Binding sitei340Shikimate-3-phosphateUniRule annotation8 Publications1
Active sitei341Proton donorUniRule annotation1 Publication1 Publication1
Binding sitei344PhosphoenolpyruvateUniRule annotation4 Publications1
Binding sitei386PhosphoenolpyruvateUniRule annotation4 Publications1
Sitei408Modified by bromopyruvate1 Publication1
Binding sitei411PhosphoenolpyruvateUniRule annotation4 Publications1
Sitei411Modified by bromopyruvate1 Publication1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10073. aroA.

Subcellular locationi

  • Cytoplasm UniRule annotationCurated

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96G → 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 Publication1
Mutagenesisi97T → 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 Publication1
Mutagenesisi101P → 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 Publications1
Mutagenesisi101P → 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 Publications1
Mutagenesisi101P → 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 Publications1
Mutagenesisi101P → 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 Publications1
Mutagenesisi313D → A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000882531 – 4273-phosphoshikimate 1-carboxyvinyltransferaseAdd BLAST427

Proteomic databases

EPDiP0A6D3.
PaxDbiP0A6D3.
PRIDEiP0A6D3.

2D gel databases

SWISS-2DPAGEP0A6D3.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi4260011. 10 interactors.
DIPiDIP-48256N.
IntActiP0A6D3. 3 interactors.
STRINGi511145.b0908.

Chemistry databases

BindingDBiP0A6D3.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi11 – 17Combined sources7
Helixi22 – 34Combined sources13
Beta strandi35 – 43Combined sources9
Helixi48 – 59Combined sources12
Beta strandi63 – 66Combined sources4
Beta strandi68 – 70Combined sources3
Beta strandi73 – 76Combined sources4
Beta strandi79 – 81Combined sources3
Beta strandi88 – 91Combined sources4
Helixi96 – 105Combined sources10
Beta strandi108 – 116Combined sources9
Helixi119 – 123Combined sources5
Helixi127 – 135Combined sources9
Beta strandi140 – 145Combined sources6
Beta strandi151 – 155Combined sources5
Beta strandi160 – 168Combined sources9
Helixi171 – 179Combined sources9
Helixi180 – 182Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi187 – 195Combined sources9
Helixi199 – 210Combined sources12
Beta strandi216 – 218Combined sources3
Turni219 – 221Combined sources3
Beta strandi222 – 225Combined sources4
Beta strandi235 – 238Combined sources4
Helixi243 – 256Combined sources14
Beta strandi257 – 264Combined sources8
Helixi272 – 275Combined sources4
Helixi276 – 283Combined sources8
Beta strandi286 – 289Combined sources4
Beta strandi291 – 297Combined sources7
Beta strandi305 – 307Combined sources3
Turni312 – 314Combined sources3
Helixi315 – 321Combined sources7
Helixi322 – 324Combined sources3
Beta strandi325 – 327Combined sources3
Beta strandi329 – 333Combined sources5
Helixi335 – 339Combined sources5
Beta strandi340 – 342Combined sources3
Helixi344 – 354Combined sources11
Beta strandi358 – 361Combined sources4
Beta strandi363 – 369Combined sources7
Helixi385 – 392Combined sources8
Helixi393 – 395Combined sources3
Beta strandi396 – 399Combined sources4
Beta strandi401 – 405Combined sources5
Helixi406 – 411Combined sources6
Helixi416 – 423Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6D3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 23Shikimate-3-phosphate bindingUniRule annotation8 Publications2
Regioni94 – 97PhosphoenolpyruvateUniRule annotation4 Publications4
Regioni169 – 171Shikimate-3-phosphate bindingUniRule annotation8 Publications3

Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
HOGENOMiHOG000247372.
InParanoidiP0A6D3.
KOiK00800.
OMAiETDHRVA.
PhylomeDBiP0A6D3.

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti23S → T in CAA25223 (Ref. 1) Curated1
Sequence conflicti330T → R in CAA25223 (Ref. 1) Curated1

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.
WP_000445231.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.
GeneIDi945528.
KEGGiecj:JW0891.
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.
WP_000445231.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4260011. 10 interactors.
DIPiDIP-48256N.
IntActiP0A6D3. 3 interactors.
STRINGi511145.b0908.

Chemistry databases

BindingDBiP0A6D3.
ChEMBLiCHEMBL5033.

2D gel databases

SWISS-2DPAGEP0A6D3.

Proteomic databases

EPDiP0A6D3.
PaxDbiP0A6D3.
PRIDEiP0A6D3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.
GeneIDi945528.
KEGGiecj:JW0891.
eco:b0908.
PATRICi32117029. VBIEscCol129921_0939.

Organism-specific databases

EchoBASEiEB0071.
EcoGeneiEG10073. aroA.

Phylogenomic databases

eggNOGiENOG4105CMY. Bacteria.
COG0128. LUCA.
HOGENOMiHOG000247372.
InParanoidiP0A6D3.
KOiK00800.
OMAiETDHRVA.
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. 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_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: November 2, 2016
This is version 103 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

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.