AC MF_00210; DC Protein; auto TR HAMAP; MF_00210; -; 1; level=0 XX Names: EPSP_synth XX ID AROA DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase; DE EC=2.5.1.19; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase; DE Short=EPSP synthase; DE Short=EPSPS; GN Name=aroA; XX 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. 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; case CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 6/7. end case case CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis. end case CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the EPSP synthase family. XX DR Pfam; PF00275; EPSP_synthase; 1; trigger=no DR PIRSF; PIRSF000505; EPSPS; 1; trigger=no DR NCBIfam; TIGR01356; AroA; 1; trigger=no DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1; trigger=no DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1; trigger=no XX KW Amino-acid biosynthesis KW Aromatic amino acid biosynthesis KW Cytoplasm KW Transferase XX GO GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity GO GO:0009073; P:aromatic amino acid family biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: AROA_ECOLI (P0A6D3) FT BINDING 22..23 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT Optional; Condition: K-S FT REGION 94..97 FT /note="Phosphoenolpyruvate" FT Optional; Condition: [LNAGDEQS]-x-[GA]-[TSIAV] FT BINDING 169..171 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT Optional; Condition: [ST]-[ST]-[QN] FT ACT_SITE 313 FT /note="Proton acceptor" FT Condition: [DE] FT ACT_SITE 341 FT /note="Proton donor" FT Condition: E FT BINDING 27 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT Condition: R FT BINDING 124 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Condition: R FT BINDING 197 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT Condition: [ST] FT BINDING 336 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT Condition: [NQ] FT BINDING 340 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT Condition: [KQ] FT BINDING 344 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Condition: R FT BINDING 386 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Condition: R FT BINDING 411 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT Condition: [KQ] XX Size: 399-469; Related: MF_03143!; Template: P0A6D3; P9WPY5; Q9R4E4; Q83E11; Q9S400; Q9KRB0; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Highly divergent AERSA; sequence not included in alignment. Divergent duplicate aroA sequence in AERPE: APE1404. Possible wrong start in SYNY3, THEMA. XX # Revision 1.48 2023/06/01 //