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Entry version 119 (08 May 2019)
Sequence version 1 (07 Jun 2005)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF), 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 1 (aroK), Shikimate kinase 2 (aroL)
  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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei27Shikimate-3-phosphateUniRule annotation7 Publications1
Binding sitei124PhosphoenolpyruvateUniRule annotation4 Publications1
Binding sitei197Shikimate-3-phosphateUniRule annotation7 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei408Modified by bromopyruvate1 Publication1
Binding sitei411PhosphoenolpyruvateUniRule annotation4 Publications1
Sitei411Modified by bromopyruvate1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:AROA-MONOMER
ECOL316407:JW0891-MONOMER
MetaCyc:AROA-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.5.1.19 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A6D3

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00053;UER00089

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:aroA1 PublicationUniRule annotation
Ordered Locus Names:b0908, JW0891
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10073 aroA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5033

Drug and drug target database

More...
DrugBanki
DB03116 5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate
DB01942 Formic Acid
DB04539 Glyphosate
DB04328 Shikimate-3-Phosphate

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000882531 – 4273-phosphoshikimate 1-carboxyvinyltransferaseAdd BLAST427

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A6D3

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6D3

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A6D3

PRoteomics IDEntifications database

More...
PRIDEi
P0A6D3

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A6D3

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260011, 10 interactors

Database of interacting proteins

More...
DIPi
DIP-48256N

Protein interaction database and analysis system

More...
IntActi
P0A6D3, 3 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0908

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A6D3

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A6D3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A6D3

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni22 – 23Shikimate-3-phosphate bindingUniRule annotation8 Publications2
Regioni94 – 97PhosphoenolpyruvateUniRule annotation4 Publications4
Regioni169 – 171Shikimate-3-phosphate bindingUniRule annotation8 Publications3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the EPSP synthase family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CMY Bacteria
COG0128 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000247372

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6D3

KEGG Orthology (KO)

More...
KOi
K00800

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6D3

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.65.10.10, 2 hits

HAMAP database of protein families

More...
HAMAPi
MF_00210 EPSP_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001986 Enolpyruvate_Tfrase_dom
IPR036968 Enolpyruvate_Tfrase_sf
IPR006264 EPSP_synthase
IPR023193 EPSP_synthase_CS
IPR013792 RNA3'P_cycl/enolpyr_Trfase_a/b

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00275 EPSP_synthase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000505 EPSPS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55205 SSF55205, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01356 aroA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00104 EPSP_SYNTHASE_1, 1 hit
PS00885 EPSP_SYNTHASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB1F55469EB4D9F97
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti23S → T in CAA25223 (Ref. 1) Curated1
Sequence conflicti330T → R in CAA25223 (Ref. 1) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
C64830 XUECVS

NCBI Reference Sequences

More...
RefSeqi
NP_415428.1, NC_000913.3
WP_000445231.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73994; AAC73994; b0908
BAA35643; BAA35643; BAA35643

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945528

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0891
eco:b0908

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1368

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
SMRiP0A6D3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP0A6D3
ChEMBLiCHEMBL5033
DrugBankiDB03116 5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate
DB01942 Formic Acid
DB04539 Glyphosate
DB04328 Shikimate-3-Phosphate

2D gel databases

SWISS-2DPAGEiP0A6D3

Proteomic databases

EPDiP0A6D3
jPOSTiP0A6D3
PaxDbiP0A6D3
PRIDEiP0A6D3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73994; AAC73994; b0908
BAA35643; BAA35643; BAA35643
GeneIDi945528
KEGGiecj:JW0891
eco:b0908
PATRICifig|1411691.4.peg.1368

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0071
EcoGeneiEG10073 aroA

Phylogenomic databases

eggNOGiENOG4105CMY Bacteria
COG0128 LUCA
HOGENOMiHOG000247372
InParanoidiP0A6D3
KOiK00800
PhylomeDBiP0A6D3

Enzyme and pathway databases

UniPathwayi
UPA00053;UER00089

BioCyciEcoCyc:AROA-MONOMER
ECOL316407:JW0891-MONOMER
MetaCyc:AROA-MONOMER
BRENDAi2.5.1.19 2026
SABIO-RKiP0A6D3

Miscellaneous databases

EvolutionaryTraceiP0A6D3

Protein Ontology

More...
PROi
PR:P0A6D3

Family and domain databases

Gene3Di3.65.10.10, 2 hits
HAMAPiMF_00210 EPSP_synth, 1 hit
InterProiView protein in InterPro
IPR001986 Enolpyruvate_Tfrase_dom
IPR036968 Enolpyruvate_Tfrase_sf
IPR006264 EPSP_synthase
IPR023193 EPSP_synthase_CS
IPR013792 RNA3'P_cycl/enolpyr_Trfase_a/b
PfamiView protein in Pfam
PF00275 EPSP_synthase, 1 hit
PIRSFiPIRSF000505 EPSPS, 1 hit
SUPFAMiSSF55205 SSF55205, 1 hit
TIGRFAMsiTIGR01356 aroA, 1 hit
PROSITEiView protein in PROSITE
PS00104 EPSP_SYNTHASE_1, 1 hit
PS00885 EPSP_SYNTHASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAROA_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A6D3
Secondary accession number(s): P07638, P78222
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: May 8, 2019
This is version 119 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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