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P0A6D3

- AROA_ECOLI

UniProt

P0A6D3 - AROA_ECOLI

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
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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 Publications

    Catalytic activityi

    Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.6 Publications

    Enzyme regulationi

    Competitively inhibited by glyphosate (PubMed:12430021, PubMed:6229418), (S)- and (R)-phosphonates analogs (PubMed:15736934), (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 Celsius. PubMed:6229418)5 Publications
    2. KM=0.015 mM for PEP (at pH 7 and 25 degrees Celsius. PubMed:6229418)5 Publications
    3. KM=0.045 mM for PEP (at pH 7.5 and 25 degrees Celsius. PubMed:19211556)5 Publications
    4. KM=0.048 mM for S3P (at pH 7.5 and 25 degrees Celsius. PubMed:19211556)5 Publications
    5. KM=0.06 mM for PEP (at pH 7.5 and 25 degrees Celsius. PubMed:17855366)5 Publications
    6. KM=0.06 mM for S3P (at pH 7.5 and 25 degrees Celsius. PubMed:17855366)5 Publications
    7. KM=0.088 mM for PEP (at pH 6.8 and 20 degrees Celsius. PubMed:12430021)5 Publications
    8. KM=0.09 mM for S3P (at pH 5.5 and 20 degrees Celsius. PubMed:16225867)5 Publications
    9. KM=0.1 mM for PEP (at pH 5.5 and 20 degrees Celsius. PubMed:16225867)5 Publications
    10. KM=0.12 mM for S3P (at pH 6.8 and 20 degrees Celsius. PubMed:12430021)5 Publications

    Vmax=50 µmol/min/µg enzyme (at pH 7.5 and 25 degrees Celsius. PubMed:17855366)5 Publications

    Vmax=53 µmol/min/µg enzyme (at pH 5.5 and 20 degrees Celsius. PubMed:16225867)5 Publications

    Vmax=57 µmol/min/µg enzyme (at pH 7.5 and 25 degrees Celsius. PubMed:19211556)5 Publications

    pH dependencei

    Optimum pH is between 6 and 6.5.5 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271Shikimate-3-phosphate5 Publications
    Binding sitei124 – 1241Phosphoenolpyruvate
    Binding sitei197 – 1971Shikimate-3-phosphate5 Publications
    Active sitei313 – 3131Proton acceptor
    Binding sitei336 – 3361Shikimate-3-phosphate5 Publications
    Binding sitei340 – 3401Shikimate-3-phosphate5 Publications
    Active sitei341 – 3411Proton donorCurated
    Binding sitei344 – 3441Phosphoenolpyruvate
    Binding sitei386 – 3861Phosphoenolpyruvate
    Sitei408 – 4081Modified by bromopyruvate
    Binding sitei411 – 4111Phosphoenolpyruvate
    Sitei411 – 4111Modified by bromopyruvate

    GO - Molecular functioni

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

    GO - Biological processi

    1. aromatic amino acid family biosynthetic process Source: UniProtKB-KW
    2. chorismate biosynthetic process Source: EcoCyc

    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-carboxyvinyltransferase (EC:2.5.1.19)
    Alternative name(s):
    5-enolpyruvylshikimate-3-phosphate synthase
    Short name:
    EPSP synthase
    Short name:
    EPSPS
    Gene namesi
    Name:aroA
    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 Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.9 Publications

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 binding
    Regioni94 – 974Phosphoenolpyruvate
    Regioni169 – 1713Shikimate-3-phosphate binding

    Sequence similaritiesi

    Belongs to the EPSP synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0128.
    HOGENOMiHOG000247372.
    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

    MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV    50
    RHMLNALTAL GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR 100
    PLAAALCLGS NDIVLTGEPR MKERPIGHLV DALRLGGAKI TYLEQENYPP 150
    LRLQGGFTGG NVDVDGSVSS QFLTALLMTA PLAPEDTVIR IKGDLVSKPY 200
    IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE GDASSASYFL 250
    AAAAIKGGTV KVTGIGRNSM QGDIRFADVL EKMGATICWG DDYISCTRGE 300
    LNAIDMDMNH IPDAAMTIAT AALFAKGTTT LRNIYNWRVK ETDRLFAMAT 350
    ELRKVGAEVE EGHDYIRITP PEKLNFAEIA TYNDHRMAMC FSLVALSDTP 400
    VTILDPKCTA KTFPDYFEQL ARISQAA 427
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 86 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