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P0A6D3

- AROA_ECOLI

UniProt

P0A6D3 - AROA_ECOLI

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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.7 PublicationsUniRule annotation

Catalytic activityi

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.7 PublicationsUniRule annotation

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

Vmax=50 µmol/min/µg enzyme (at pH 7.5 and 25 degrees Celsius1 Publication

Vmax=53 µmol/min/µg enzyme (at pH 5.5 and 20 degrees Celsius1 Publication

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271Shikimate-3-phosphate7 PublicationsUniRule annotation
Binding sitei124 – 1241Phosphoenolpyruvate4 PublicationsUniRule annotation
Binding sitei197 – 1971Shikimate-3-phosphate7 PublicationsUniRule annotation
Active sitei313 – 3131Proton acceptor7 PublicationsUniRule annotation
Binding sitei336 – 3361Shikimate-3-phosphate7 PublicationsUniRule annotation
Binding sitei340 – 3401Shikimate-3-phosphate8 PublicationsUniRule annotation
Active sitei341 – 3411Proton donor1 Publication1 PublicationUniRule annotation
Binding sitei344 – 3441Phosphoenolpyruvate4 PublicationsUniRule annotation
Binding sitei386 – 3861Phosphoenolpyruvate4 PublicationsUniRule annotation
Sitei408 – 4081Modified by bromopyruvate1 Publication
Binding sitei411 – 4111Phosphoenolpyruvate4 PublicationsUniRule annotation
Sitei411 – 4111Modified by bromopyruvate1 Publication

GO - Molecular functioni

  1. 3-phosphoshikimate 1-carboxyvinyltransferase activity Source: UniProtKB

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-KW
  2. chorismate biosynthetic process Source: EcoCyc
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.
SABIO-RKP0A6D3.
UniPathwayiUPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.196 PublicationsUniRule annotation)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase1 PublicationUniRule annotation
Short name:
EPSP synthase1 PublicationUniRule annotation
Short name:
EPSPSCuratedUniRule annotation
Gene namesi
Name:aroA1 PublicationUniRule annotation
Ordered Locus Names:b0908, JW0891
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10073. aroA.

Subcellular locationi

Cytoplasm CuratedUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi96 – 961G → 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 Publication
Mutagenesisi97 – 971T → 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 Publication
Mutagenesisi101 – 1011P → 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 Publications
Mutagenesisi101 – 1011P → 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 Publications
Mutagenesisi101 – 1011P → 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 Publications
Mutagenesisi101 – 1011P → 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 Publications
Mutagenesisi313 – 3131D → A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4274273-phosphoshikimate 1-carboxyvinyltransferasePRO_0000088253Add
BLAST

Proteomic databases

PaxDbiP0A6D3.
PRIDEiP0A6D3.

2D gel databases

SWISS-2DPAGEP0A6D3.

Expressioni

Gene expression databases

GenevestigatoriP0A6D3.

Interactioni

Subunit structurei

Monomer.1 PublicationUniRule annotation

Protein-protein interaction databases

DIPiDIP-48256N.
IntActiP0A6D3. 3 interactions.
STRINGi511145.b0908.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi11 – 177Combined sources
Helixi22 – 3413Combined sources
Beta strandi35 – 439Combined sources
Helixi48 – 5912Combined sources
Beta strandi63 – 664Combined sources
Beta strandi68 – 703Combined sources
Beta strandi73 – 764Combined sources
Beta strandi79 – 813Combined sources
Beta strandi88 – 914Combined sources
Helixi96 – 10510Combined sources
Beta strandi108 – 1169Combined sources
Helixi119 – 1235Combined sources
Helixi127 – 1359Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi160 – 1689Combined sources
Helixi171 – 1799Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi187 – 1959Combined sources
Helixi199 – 21012Combined sources
Beta strandi216 – 2183Combined sources
Turni219 – 2213Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi235 – 2384Combined sources
Helixi243 – 25614Combined sources
Beta strandi257 – 2648Combined sources
Helixi272 – 2754Combined sources
Helixi276 – 2838Combined sources
Beta strandi286 – 2894Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi305 – 3073Combined sources
Turni312 – 3143Combined sources
Helixi315 – 3217Combined sources
Helixi322 – 3243Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi329 – 3335Combined sources
Helixi335 – 3395Combined sources
Beta strandi340 – 3423Combined sources
Helixi344 – 35411Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi363 – 3697Combined sources
Helixi385 – 3928Combined sources
Helixi393 – 3953Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi401 – 4055Combined sources
Helixi406 – 4116Combined sources
Helixi416 – 4238Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6D3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 232Shikimate-3-phosphate binding8 PublicationsUniRule annotation
Regioni94 – 974Phosphoenolpyruvate4 PublicationsUniRule annotation
Regioni169 – 1713Shikimate-3-phosphate binding8 PublicationsUniRule annotation

Sequence similaritiesi

Belongs to the EPSP synthase family.CuratedUniRule annotation

Phylogenomic databases

eggNOGiCOG0128.
HOGENOMiHOG000247372.
InParanoidiP0A6D3.
KOiK00800.
OMAiGADIEWG.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP0A6D3.

Family and domain databases

Gene3Di3.65.10.10. 2 hits.
HAMAPiMF_00210. EPSP_synth.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231S → T in CAA25223. 1 PublicationCurated
Sequence conflicti330 – 3301T → R in CAA25223. 1 PublicationCurated

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.
YP_489180.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73994; AAC73994; b0908.
BAA35643; BAA35643; BAA35643.
GeneIDi12931017.
945528.
KEGGiecj:Y75_p0880.
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 .
PIRi C64830. XUECVS.
RefSeqi NP_415428.1. NC_000913.3.
YP_489180.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EPS X-ray 3.00 A 1-427 [» ]
1G6S X-ray 1.50 A 1-427 [» ]
1G6T X-ray 1.60 A 1-427 [» ]
1MI4 X-ray 1.70 A 1-427 [» ]
1P88 NMR - A 25-240 [» ]
1P89 NMR - A 25-240 [» ]
1Q0I model - A 1-427 [» ]
1Q0J model - A 1-427 [» ]
1Q36 X-ray 1.60 A 1-427 [» ]
1X8R X-ray 1.50 A 1-427 [» ]
1X8T X-ray 1.90 A 1-427 [» ]
2AA9 X-ray 1.50 A 1-427 [» ]
2AAY X-ray 1.55 A 1-427 [» ]
2PQ9 X-ray 1.60 A 1-427 [» ]
2QFQ X-ray 1.50 A 1-427 [» ]
2QFS X-ray 1.55 A 1-427 [» ]
2QFT X-ray 1.55 A 1-427 [» ]
2QFU X-ray 1.60 A 1-427 [» ]
3FJX X-ray 1.75 A 1-427 [» ]
3FJZ X-ray 1.70 A 1-427 [» ]
3FK0 X-ray 1.70 A 1-427 [» ]
3FK1 X-ray 1.70 A 1-427 [» ]
ProteinModelPortali P0A6D3.
SMRi P0A6D3. Positions 1-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48256N.
IntActi P0A6D3. 3 interactions.
STRINGi 511145.b0908.

Chemistry

BindingDBi P0A6D3.
ChEMBLi CHEMBL5033.

2D gel databases

SWISS-2DPAGE P0A6D3.

Proteomic databases

PaxDbi P0A6D3.
PRIDEi P0A6D3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73994 ; AAC73994 ; b0908 .
BAA35643 ; BAA35643 ; BAA35643 .
GeneIDi 12931017.
945528.
KEGGi ecj:Y75_p0880.
eco:b0908.
PATRICi 32117029. VBIEscCol129921_0939.

Organism-specific databases

EchoBASEi EB0071.
EcoGenei EG10073. aroA.

Phylogenomic databases

eggNOGi COG0128.
HOGENOMi HOG000247372.
InParanoidi P0A6D3.
KOi K00800.
OMAi GADIEWG.
OrthoDBi EOG6Z6FZ4.
PhylomeDBi P0A6D3.

Enzyme and pathway databases

UniPathwayi UPA00053 ; UER00089 .
BioCyci EcoCyc:AROA-MONOMER.
ECOL316407:JW0891-MONOMER.
MetaCyc:AROA-MONOMER.
SABIO-RK P0A6D3.

Miscellaneous databases

EvolutionaryTracei P0A6D3.
PROi P0A6D3.

Gene expression databases

Genevestigatori P0A6D3.

Family and domain databases

Gene3Di 3.65.10.10. 2 hits.
HAMAPi MF_00210. EPSP_synth.
InterProi IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view ]
Pfami PF00275. EPSP_synthase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000505. EPSPS. 1 hit.
SUPFAMi SSF55205. SSF55205. 1 hit.
TIGRFAMsi TIGR01356. aroA. 1 hit.
PROSITEi PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-427.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain of Escherichia coli."
    Duncan K., Lewendon A., Coggins J.R.
    FEBS Lett. 165:121-127(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
  7. "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: ENZYME REGULATION.
  8. "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.
  9. "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).
  10. "Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail."
    Schonbrunn E., Eschenburg S., Shuttleworth W.A., Schloss J.V., Amrhein N., Evans J.N., Kabsch W.
    Proc. Natl. Acad. Sci. U.S.A. 98:1376-1380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOG.
  11. "How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli."
    Eschenburg S., Healy M.L., Priestman M.A., Lushington G.H., Schonbrunn E.
    Planta 216:129-135(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-96 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-96, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  12. "A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states."
    Eschenburg S., Kabsch W., Healy M.L., Schonbrunn E.
    J. Biol. Chem. 278:49215-49222(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANT ALA-313 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-313, ACTIVE SITE, REACTION MECHANISM.
  13. "Letter: Substrate-induced structural changes to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase."
    Young J.K., Stauffer M.E., Kim H.J., Helms G.L., Evans J.N.S.
    Submitted (MAY-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 25-240.
  14. "Interaction of phosphonate analogues of the tetrahedral reaction intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic detail."
    Priestman M.A., Healy M.L., Becker A., Alberg D.G., Bartlett P.A., Lushington G.H., Schonbrunn E.
    Biochemistry 44:3241-3248(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOGS, ENZYME REGULATION, ACTIVE SITE, REACTION MECHANISM.
  15. "Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate."
    Priestman M.A., Healy M.L., Funke T., Becker A., Schonbrunn E.
    FEBS Lett. 579:5773-5780(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  16. "Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-phosphate synthases by tetrahedral reaction intermediate analogues."
    Funke T., Healy-Fried M.L., Han H., Alberg D.G., Bartlett P.A., Schonbrunn E.
    Biochemistry 46:13344-13351(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOGS, FUNCTION, ACTIVE SITE, ENZYME REGULATION.
  17. "Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase."
    Healy-Fried M.L., Funke T., Priestman M.A., Han H., Schonbrunn E.
    J. Biol. Chem. 282:32949-32955(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS L101 AND S101 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PRO-101, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.
  18. "Structural basis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli."
    Funke T., Yang Y., Han H., Healy-Fried M., Olesen S., Becker A., Schonbrunn E.
    J. Biol. Chem. 284:9854-9860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-97 AND PRO-101, BIOPHYSICOCHEMICAL PROPERTIES.

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 26, 2014
This is version 88 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

External Data

Dasty 3