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AROA_STRTD
ID   AROA_STRTD              Reviewed;         427 AA.
AC   Q03LG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=STER_0695;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR   EMBL; CP000419; ABJ65953.1; -; Genomic_DNA.
DR   RefSeq; WP_011680947.1; NC_008532.1.
DR   AlphaFoldDB; Q03LG9; -.
DR   SMR; Q03LG9; -.
DR   KEGG; ste:STER_0695; -.
DR   HOGENOM; CLU_024321_0_1_9; -.
DR   OMA; YEDHRMA; -.
DR   UniPathway; UPA00053; UER00089.
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:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01556; EPSP_synthase; 1.
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_1000012501"
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         20..21
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         25
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         120
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
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         385
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   427 AA;  45922 MW;  4E6DF3C048F4E016 CRC64;
     MKLETKAQGL RGSLRIPGDK SISHRSIMFG SLAKGVTTVR DILRGEDVLS TMQVFRDLGV
     TIEDDGDVVR IHGVGFDGLK APQNKLDMGN SGTSIRLISG VLAGQDFDVE MFGDDSLSKR
     PMDRVTIPLR QMGVEVSGQT DRDLPPLKMH GSKSLKPIYY ELPVASAQVK SALIFAALQA
     DGESVIIEKE KTRNHTEDMI QQFGGQLQVE GKEIRISGGQ TFTAQEVVVP GDISSAAFWL
     VAGLVVPNSK IVLKNVGINE TRTGIIDVIK NMGGKIKLSD IDQVAKSATI TVETSELNGT
     EIGGDIIPRL IDELPIITLL ATQAQGKTVI RDAEELKVKE TDRIQVVADA LNAMGADIVP
     TEDGMIITGK TPLHGAEVNT FGDHRIGMMT AIAALLVQDG EVDLQRAEAI NTSYPSFFSD
     LEGLLHG
 
 
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