ID   AROA_ACIC1              Reviewed;         423 AA.
AC   A0LS98;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   04-NOV-2026, entry version 109.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210};
DE            EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE            Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210};
GN   OrderedLocusNames=Acel_0535;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales;
OC   Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC       phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate
CC       (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00210};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21257;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00210};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00210}.
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DR   EMBL; CP000481; ABK52308.1; -; Genomic_DNA.
DR   RefSeq; WP_011719371.1; NC_008578.1.
DR   AlphaFoldDB; A0LS98; -.
DR   SMR; A0LS98; -.
DR   FunCoup; A0LS98; 209.
DR   STRING; 351607.Acel_0535; -.
DR   KEGG; ace:Acel_0535; -.
DR   eggNOG; COG0128; Bacteria.
DR   HOGENOM; CLU_024321_0_0_11; -.
DR   InParanoid; A0LS98; -.
DR   OMA; AACFCDG; -.
DR   OrthoDB; 9809920at2; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   FunFam; 3.65.10.10:FF:000010; 3-phosphoshikimate 1-carboxyvinyltransferase; 1.
DR   FunFam; 3.65.10.10:FF:000011; 3-phosphoshikimate 1-carboxyvinyltransferase; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   NCBIfam; TIGR01356; aroA; 1.
DR   PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   PIRSF; PIRSF000505; EPSPS; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN           1..423
FT                   /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT                   /id="PRO_1000099658"
FT   ACT_SITE        312
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         28
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         28
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         29
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         33
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         96
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         124
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         169
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         170
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         171
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         171
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         198
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         312
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         339
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         343
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         384
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         409
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   423 AA;  44002 MW;  646E607EBB8EC075 CRC64;
     MTTTELTGWP APTASGRVDA VVHLPGSKSM TNRALVLAAL AAEPTAIRGG LRARDTELMM
     AGLRSLGVGI DDAGDMWLVS PAELRGPAAI DCGLAGTVMR FLLAAATLAT GEVSFDGDPR
     ARERPLRPLL DALRQLGAEL RDTGGRLPVT VVGSGHLPGG HCVVDASASS QFVSALLLVA
     PRADTPVTVG HVGRTLPSVP HITMTVAMLR ERGVEVAGTD GSWRVQPGPI RGGTVQIEPD
     LSNAAPFLAA ALVTGGRVRV PDWPMRTTQA GDALRDLLTA MGARCELDAT GLTVTGGPVI
     HGLDADLRDV SELVPTLAAL AALADRPSTF RGIGHMRGHE TDRLAALAAE LTRLGGDVTA
     TDDGLVIRPR PLHGGVFHSY GDHRMATTGA VLGLVIPGIV VENIQTVAKT MPTFVELWTG
     MLR
//