AROA_ENTFO
ID AROA_ENTFO Reviewed; 426 AA.
AC F2MTI3; Q7C3L6; Q9ANY6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 48.
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=OG1RF_11285;
OS Enterococcus faecalis (strain ATCC 47077 / OG1RF).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=474186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RA Huycke M.M., Shepard L., Joyce W., Wise P., Moore D.R., Gilmore M.S.;
RT "Forme fruste respiration by Enterococcus faecalis produces extracellular
RT superoxide.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=18611278; DOI=10.1186/gb-2008-9-7-r110;
RA Bourgogne A., Garsin D.A., Qin X., Singh K.V., Sillanpaa J.,
RA Yerrapragada S., Ding Y., Dugan-Rocha S., Buhay C., Shen H., Chen G.,
RA Williams G., Muzny D., Maadani A., Fox K.A., Gioia J., Chen L., Shang Y.,
RA Arias C.A., Nallapareddy S.R., Zhao M., Prakash V.P., Chowdhury S.,
RA Jiang H., Gibbs R.A., Murray B.E., Highlander S.K., Weinstock G.M.;
RT "Large scale variation in Enterococcus faecalis illustrated by the genome
RT analysis of strain OG1RF.";
RL Genome Biol. 9:R110.1-R110.16(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG53678.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEA93972.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF318277; AAG53678.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002621; AEA93972.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; F2MTI3; -.
DR SMR; F2MTI3; -.
DR KEGG; efi:OG1RF_11285; -.
DR HOGENOM; CLU_024321_0_1_9; -.
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..426
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000412115"
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"
FT CONFLICT 74
FT /note="Q -> R (in Ref. 1; AAG53678)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> A (in Ref. 1; AAG53678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 45448 MW; 92A50F893FB2235F CRC64;
MQLRTNVKHL QGTLMVPSDK SISHRSIMFG AISSGKTTIT NFLRGEDCLS TLAAFRSLGV
NIEDDGTTIT VEGQGFAGLK KAKNTIDVGN SGTTIRLMLG ILAGCPFETR LAGDASISKR
PMNRVMLPLN QMGAECQGVQ QTEFPPISIR GTQNLQPIDY TMPVASAQVK SAILFAALQA
EGTSVVVEKE KTRDHTEEMI RQFGGTLEVD GKKIMLTGPQ QLTGQNVVVP GDISSAAFFL
VAGLVVPDSE ILLKNVGLNQ TRTGILDVIK NMGGSVTILN EDEANHSGDL LVKTSQLTAT
EIGGAIIPRL IDELPIIALL ATQATGTTII RDAEELKVKE TNRIDAVAKE LTILGADITP
TDDGLIIHGP TSLHGGRVTS YGDHRIGMML QIAALLVKEG TVELDKAEAV SVSYPAFFDD
LERLSC
