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P0A6D3 (AROA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-phosphoshikimate 1-carboxyvinyltransferase

EC=2.5.1.19
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase
Short name=EPSP synthase
Short name=EPSPS
Gene names
Name:aroA
Ordered Locus Names:b0908, JW0891
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. HAMAP-Rule MF_00210

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. HAMAP-Rule MF_00210

Subunit structure

Monomer.

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00210.

Sequence similarities

Belongs to the EPSP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4274273-phosphoshikimate 1-carboxyvinyltransferase HAMAP-Rule MF_00210
PRO_0000088253

Sites

Site4081Modified by bromopyruvate
Site4111Modified by bromopyruvate

Natural variations

Natural variant961G → A Confers glyphosate inhibition.

Experimental info

Sequence conflict231S → T in CAA25223. Ref.1
Sequence conflict3301T → R in CAA25223. Ref.1

Secondary structure

..................................................................................... 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6D3 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: B1F55469EB4D9F97

FASTA42746,096
        10         20         30         40         50         60 
MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV RHMLNALTAL 

        70         80         90        100        110        120 
GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR PLAAALCLGS NDIVLTGEPR 

       130        140        150        160        170        180 
MKERPIGHLV DALRLGGAKI TYLEQENYPP LRLQGGFTGG NVDVDGSVSS QFLTALLMTA 

       190        200        210        220        230        240 
PLAPEDTVIR IKGDLVSKPY IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE 

       250        260        270        280        290        300 
GDASSASYFL AAAAIKGGTV KVTGIGRNSM QGDIRFADVL EKMGATICWG DDYISCTRGE 

       310        320        330        340        350        360 
LNAIDMDMNH IPDAAMTIAT AALFAKGTTT LRNIYNWRVK ETDRLFAMAT ELRKVGAEVE 

       370        380        390        400        410        420 
EGHDYIRITP PEKLNFAEIA TYNDHRMAMC FSLVALSDTP VTILDPKCTA KTFPDYFEQL 


ARISQAA 

« Hide

References

« Hide 'large scale' references
[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]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]Palma C.A., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M., Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Kim K., Komp C., Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-427.
Strain: K12 / MG1655 / ATCC 47076.
[6]"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: INHIBITION BY BROMOPYRUVATE.
[7]"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.
[8]"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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00557 Genomic DNA. Translation: CAA25223.1.
U00096 Genomic DNA. Translation: AAC73994.1.
AP009048 Genomic DNA. Translation: BAA35643.1.
U31523 Genomic DNA. Translation: AAA81514.1.
PIRXUECVS. C64830.
RefSeqNP_415428.1. NC_000913.3.
YP_489180.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A6D3.
SMRP0A6D3. Positions 1-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48256N.
IntActP0A6D3. 3 interactions.
STRING511145.b0908.

Chemistry

BindingDBP0A6D3.
ChEMBLCHEMBL5033.

2D gel databases

SWISS-2DPAGEP0A6D3.

Proteomic databases

PaxDbP0A6D3.
PRIDEP0A6D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.
GeneID12931017.
945528.
KEGGecj:Y75_p0880.
eco:b0908.
PATRIC32117029. VBIEscCol129921_0939.

Organism-specific databases

EchoBASEEB0071.
EcoGeneEG10073. aroA.

Phylogenomic databases

eggNOGCOG0128.
HOGENOMHOG000247372.
KOK00800.
OMAGADIEWG.
OrthoDBEOG6Z6FZ4.
PhylomeDBP0A6D3.
ProtClustDBPRK02427.

Enzyme and pathway databases

BioCycEcoCyc:AROA-MONOMER.
ECOL316407:JW0891-MONOMER.
MetaCyc:AROA-MONOMER.
SABIO-RKP0A6D3.
UniPathwayUPA00053; UER00089.

Gene expression databases

GenevestigatorP0A6D3.

Family and domain databases

Gene3D3.65.10.10. 2 hits.
HAMAPMF_00210. EPSP_synth.
InterProIPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PfamPF00275. EPSP_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000505. EPSPS. 1 hit.
SUPFAMSSF55205. SSF55205. 1 hit.
TIGRFAMsTIGR01356. aroA. 1 hit.
PROSITEPS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6D3.
PROP0A6D3.

Entry information

Entry nameAROA_ECOLI
AccessionPrimary (citable) accession number: P0A6D3
Secondary accession number(s): P07638, P78222
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene