ID AROA_STRP2 Reviewed; 427 AA. AC Q04JX6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 02-DEC-2020, entry version 89. 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}; OrderedLocusNames=SPD_1205; OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=373153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D39 / NCTC 7466; RX PubMed=17041037; DOI=10.1128/jb.01148-06; RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.; RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus RT pneumoniae and comparison with that of unencapsulated laboratory strain RT R6."; RL J. Bacteriol. 189:38-51(2007). 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000410; ABJ54185.1; -; Genomic_DNA. DR RefSeq; WP_001819694.1; NC_008533.2. DR SMR; Q04JX6; -. DR STRING; 373153.SPD_1205; -. DR EnsemblBacteria; ABJ54185; ABJ54185; SPD_1205. DR KEGG; spd:SPD_1205; -. DR eggNOG; COG0128; Bacteria. DR HOGENOM; CLU_024321_0_1_9; -. DR OMA; YEDHRMA; -. DR OrthoDB; 533829at2; -. DR BioCyc; SPNE373153:G1G6V-1303-MONOMER; -. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000001452; 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 family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.65.10.10; -; 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 Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01356; aroA; 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 Transferase. FT CHAIN 1..427 FT /note="3-phosphoshikimate 1-carboxyvinyltransferase" FT /id="PRO_1000012490" FT REGION 20..21 FT /note="Shikimate-3-phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT REGION 90..93 FT /note="Phosphoenolpyruvate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT ACT_SITE 312 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT ACT_SITE 340 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT BINDING 25 FT /note="Shikimate-3-phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT BINDING 120 FT /note="Phosphoenolpyruvate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT BINDING 339 FT /note="Shikimate-3-phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT BINDING 343 FT /note="Phosphoenolpyruvate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" FT BINDING 385 FT /note="Phosphoenolpyruvate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210" SQ SEQUENCE 427 AA; 45720 MW; D48A60F444E45818 CRC64; MKLKTNIRHL HGSIRVPGDK SISHRSIIFG SLAEGETKVY DILRGEDVLS TMQVFRDLGV EIEDKDGVIT IQGVGMAGLK APQNALNMGN SGTSIRLISG VLAGADFEVE MFGDDSLSKR PMDRVTLPLK KMGVSISGQT ERDLPPLRLK GTKNLRPIHY ELPIASAQVK SALMFAALQA KGESVIIEKE CTRNHTEDML KQFGGHLSVD GKKITVQGPQ KLTGQKVVVP GDISSAAFWL VAGLINPNSH LVLQNVGINE TRTGIIDVIR AMGGKLEVTE IDPVAKSSTL TVESSDLKGT EIGGALIPRL IDELPIIALL ATQAQGVTVI KDAEELKVKE TDRIQVVADA LNSMGADITP TADGMIIKGK SALHGARVNT FGDHRIGMMT AIAALLVADG EVELDRAEAI NTSYPSFFDD LESLIHG //