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Protein

3-phosphoshikimate 1-carboxyvinyltransferase

Gene

aroA

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
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 annotation2 Publications

Catalytic activityi

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.UniRule annotation1 Publication

Enzyme regulationi

Competitively inhibited by glyphosate. Avtivated by ammonium, rubidium or potassium ions.1 Publication

Kineticsi

  1. KM=22 µM for PEP (with 100 mM ammonium at pH 7 and 25 degrees Celsius)1 Publication
  2. KM=31 µM for S3P (with 100 mM ammonium at pH 7 and 25 degrees Celsius)1 Publication
  3. KM=91 µM for PEP (with 10 mM ammonium at pH 7 and 25 degrees Celsius)1 Publication
  4. KM=100 µM for PEP (with 1 mM ammonium at pH 7 and 25 degrees Celsius)1 Publication
  5. KM=118 µM for S3P (with 10 mM ammonium at pH 7 and 25 degrees Celsius)1 Publication
  6. KM=145 µM for S3P (with 1 mM ammonium at pH 7 and 25 degrees Celsius)1 Publication

    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 (SP_1700), Phospho-2-dehydro-3-deoxyheptonate aldolase (SP_1701)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroD)
    4. Shikimate dehydrogenase (NADP(+)) (aroE)
    5. Shikimate kinase (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 sitei25Shikimate-3-phosphateUniRule annotation1 Publication1
    Binding sitei120PhosphoenolpyruvateUniRule annotation1
    Active sitei312Proton acceptorUniRule annotation1 Publication1
    Binding sitei339Shikimate-3-phosphateUniRule annotation1 Publication1
    Active sitei340Proton donorUniRule annotation1
    Binding sitei343PhosphoenolpyruvateUniRule annotation1
    Binding sitei385PhosphoenolpyruvateUniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Enzyme and pathway databases

    BRENDAi2.5.1.19. 1960.
    SABIO-RKQ9S400.
    UniPathwayiUPA00053; UER00089.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.19UniRule annotation1 Publication)
    Alternative name(s):
    5-enolpyruvylshikimate-3-phosphate synthase1 PublicationUniRule annotation
    Short name:
    EPSP synthaseUniRule annotation
    Short name:
    EPSPSUniRule annotation
    Gene namesi
    Name:aroAUniRule annotation
    Ordered Locus Names:SP_1371
    OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
    Taxonomic identifieri170187 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    Proteomesi
    • UP000000585 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000883041 – 4273-phosphoshikimate 1-carboxyvinyltransferaseAdd BLAST427

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    enoQ97QS22EBI-2207276,EBI-2207206
    gatCQ97SE52EBI-2207276,EBI-2207053
    groSQ97NV32EBI-2207276,EBI-2206949

    Protein-protein interaction databases

    IntActiQ9S400. 3 interactors.
    STRINGi170187.SpneT_02001692.

    Structurei

    Secondary structure

    1427
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 14Combined sources5
    Helixi20 – 32Combined sources13
    Beta strandi33 – 41Combined sources9
    Helixi46 – 57Combined sources12
    Beta strandi61 – 65Combined sources5
    Beta strandi68 – 72Combined sources5
    Beta strandi86 – 89Combined sources4
    Helixi92 – 101Combined sources10
    Helixi102 – 104Combined sources3
    Beta strandi106 – 112Combined sources7
    Helixi117 – 119Combined sources3
    Helixi123 – 131Combined sources9
    Beta strandi135 – 139Combined sources5
    Turni140 – 143Combined sources4
    Beta strandi144 – 150Combined sources7
    Beta strandi159 – 161Combined sources3
    Helixi167 – 177Combined sources11
    Beta strandi180 – 187Combined sources8
    Helixi195 – 202Combined sources8
    Beta strandi208 – 210Combined sources3
    Beta strandi213 – 218Combined sources6
    Beta strandi226 – 228Combined sources3
    Helixi233 – 245Combined sources13
    Beta strandi249 – 257Combined sources9
    Turni260 – 262Combined sources3
    Helixi264 – 271Combined sources8
    Beta strandi275 – 282Combined sources8
    Turni283 – 286Combined sources4
    Beta strandi287 – 293Combined sources7
    Turni304 – 306Combined sources3
    Helixi307 – 309Combined sources3
    Helixi311 – 313Combined sources3
    Helixi314 – 322Combined sources9
    Beta strandi324 – 330Combined sources7
    Helixi334 – 338Combined sources5
    Beta strandi339 – 341Combined sources3
    Helixi345 – 352Combined sources8
    Turni353 – 355Combined sources3
    Beta strandi358 – 361Combined sources4
    Beta strandi364 – 369Combined sources6
    Beta strandi376 – 379Combined sources4
    Helixi384 – 395Combined sources12
    Beta strandi398 – 400Combined sources3
    Beta strandi402 – 405Combined sources4
    Helixi407 – 412Combined sources6
    Helixi417 – 424Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1RF4X-ray2.20A/B/C/D1-427[»]
    1RF5X-ray2.30A/B/C/D1-427[»]
    1RF6X-ray1.90A/B/C/D1-427[»]
    ProteinModelPortaliQ9S400.
    SMRiQ9S400.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S400.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni20 – 21Shikimate-3-phosphate bindingUniRule annotation1 Publication2
    Regioni90 – 93Phosphoenolpyruvate bindingUniRule annotation4

    Sequence similaritiesi

    Belongs to the EPSP synthase family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105CMY. Bacteria.
    COG0128. LUCA.
    HOGENOMiHOG000247371.
    KOiK00800.
    OMAiETDHRVA.

    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.

    Q9S400-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLKTNIRHL HGSIRVPGDK SISHRSIIFG SLAEGETKVY DILRGEDVLS
    60 70 80 90 100
    TMQVFRDLGV EIEDKDGVIT IQGVGMAGLK APQNALNMGN SGTSIRLISG
    110 120 130 140 150
    VLAGADFEVE MFGDDSLSKR PMDRVTLPLK KMGVSISGQT ERDLPPLRLK
    160 170 180 190 200
    GTKNLRPIHY ELPIASAQVK SALMFAALQA KGESVIIEKE YTRNHTEDML
    210 220 230 240 250
    KQFGGHLSVD GKKITVQGPQ KLTGQKVVVP GDISSAAFWL VAGLIAPNSR
    260 270 280 290 300
    LVLQNVGINE TRTGIIDVIR AMGGKLEITE IDPVAKSATL IVESSDLKGT
    310 320 330 340 350
    EIGGALIPRL IDELPIIALL ATQAQGVTVI KDAEELKVKE TDRIQVVADA
    360 370 380 390 400
    LNSMGADITP TADGMIIKGK SALHGARVNT FGDHRIGMMT AIAALLVADG
    410 420
    EVELDRAEAI NTSYPSFFDD LESLIHG
    Length:427
    Mass (Da):45,766
    Last modified:September 26, 2001 - v2
    Checksum:i45CE6F4D0D1C7B70
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti13S → I in AAD45819 (PubMed:10601870).Curated1
    Sequence conflicti71I → V in AAD45819 (PubMed:10601870).Curated1
    Sequence conflicti201K → Q in AAD45819 (PubMed:10601870).Curated1
    Sequence conflicti303G → C in AAD45819 (PubMed:10601870).Curated1

    Mass spectrometryi

    Molecular mass is 45825 Da from positions 1 - 427. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF169483 Genomic DNA. Translation: AAD45819.1.
    AE005672 Genomic DNA. Translation: AAK75469.1.
    PIRiD95159.
    RefSeqiWP_001808726.1. NZ_AKVY01000001.1.

    Genome annotation databases

    EnsemblBacteriaiAAK75469; AAK75469; SP_1371.
    KEGGispn:SP_1371.
    PATRICi19707147. VBIStrPne105772_1416.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF169483 Genomic DNA. Translation: AAD45819.1.
    AE005672 Genomic DNA. Translation: AAK75469.1.
    PIRiD95159.
    RefSeqiWP_001808726.1. NZ_AKVY01000001.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1RF4X-ray2.20A/B/C/D1-427[»]
    1RF5X-ray2.30A/B/C/D1-427[»]
    1RF6X-ray1.90A/B/C/D1-427[»]
    ProteinModelPortaliQ9S400.
    SMRiQ9S400.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9S400. 3 interactors.
    STRINGi170187.SpneT_02001692.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK75469; AAK75469; SP_1371.
    KEGGispn:SP_1371.
    PATRICi19707147. VBIStrPne105772_1416.

    Phylogenomic databases

    eggNOGiENOG4105CMY. Bacteria.
    COG0128. LUCA.
    HOGENOMiHOG000247371.
    KOiK00800.
    OMAiETDHRVA.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00089.
    BRENDAi2.5.1.19. 1960.
    SABIO-RKQ9S400.

    Miscellaneous databases

    EvolutionaryTraceiQ9S400.

    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_STRPN
    AccessioniPrimary (citable) accession number: Q9S400
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 26, 2001
    Last modified: November 2, 2016
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.