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 08-FEB-2011, entry version 36. 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; OrderedLocusNames=SPD_1205; OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466). OC Bacteria; Firmicutes; 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., RA Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.; RT "Genome sequence of Avery's virulent serotype 2 strain D39 of RT Streptococcus pneumoniae and comparison with that of unencapsulated RT laboratory strain R6."; RL J. Bacteriol. 189:38-51(2007). CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the EPSP synthase family. 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; YP_816672.1; NC_008533.1. DR ProteinModelPortal; Q04JX6; -. DR SMR; Q04JX6; 1-427. DR STRING; Q04JX6; -. DR EnsemblBacteria; EBSTRT00000019476; EBSTRP00000018716; EBSTRG00000019476. DR GeneID; 4441387; -. DR GenomeReviews; CP000410_GR; SPD_1205. DR KEGG; spd:SPD_1205; -. DR eggNOG; COG0128; -. DR GeneTree; EBGT00050000028044; -. DR HOGENOM; HBG646626; -. DR OMA; LSRNHTE; -. DR ProtClustDB; PRK02427; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:EC. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00210; EPSP_synth; 1; -. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR006264; EPSP_synthase. DR InterPro; IPR023193; EPSP_synthase_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR Gene3D; G3DSA:3.65.10.10; EPSP_synthase; 2. DR Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 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; KW Complete proteome; Cytoplasm; Transferase. FT CHAIN 1 427 3-phosphoshikimate 1- FT carboxyvinyltransferase. FT /FTId=PRO_1000012490. 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 //