AROA_STAA8
ID AROA_STAA8 Reviewed; 432 AA.
AC Q05615; Q2FYH1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
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};
GN OrderedLocusNames=SAOUHSC_01481;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8371108; DOI=10.1099/00221287-139-7-1449;
RA O'Connell C.M., Pattee P., Foster T.J.;
RT "Sequence and mapping of the aroA gene of Staphylococcus aureus 8325-4.";
RL J. Gen. Microbiol. 139:1449-1460(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (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, ECO:0000305}.
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; L05004; AAA71897.1; -; Unassigned_DNA.
DR EMBL; CP000253; ABD30566.1; -; Genomic_DNA.
DR RefSeq; WP_000245895.1; NZ_LS483365.1.
DR RefSeq; YP_499999.1; NC_007795.1.
DR AlphaFoldDB; Q05615; -.
DR SMR; Q05615; -.
DR STRING; 1280.SAXN108_1487; -.
DR EnsemblBacteria; ABD30566; ABD30566; SAOUHSC_01481.
DR GeneID; 3920236; -.
DR KEGG; sao:SAOUHSC_01481; -.
DR PATRIC; fig|93061.5.peg.1350; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_9; -.
DR OMA; YEDHRMA; -.
DR UniPathway; UPA00053; UER00089.
DR PRO; PR:Q05615; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Reference proteome; Transferase.
FT CHAIN 1..432
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088295"
FT REGION 93..96
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 345
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 23..24
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 28
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 123
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 344
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 348
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 390
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT CONFLICT 60
FT /note="L -> H (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..82
FT /note="SF -> V (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="I -> N (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="P -> Q (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..385
FT /note="VDS -> DI (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="SL -> CV (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="E -> Q (in Ref. 1; AAA71897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47003 MW; 7C092783DC8E3F5F CRC64;
MVNEQIIDIS GPLKGEIEVP GDKSMTHRAI MLASLAEGVS TIYKPLLGED CRRTMDIFRL
LGVEIKEDDE KLVVTSPGYQ SFNTPHQVLY TGNSGTTTRL LAGLLSGLGI ESVLSGDVSI
GKRPMDRVLR PLKLMDANIE GIEDNYTPLI IKPSVIKGIN YQMEVASAQV KSAILFASLF
SKEPTIIKEL DVSRNHTETM FKHFNIPIEA EGLSINTTPE AIRYIKPADF HVPGDISSAA
FFIVAALITP GSDVTIHNVG INPTRSGIID IVEKMGGNIQ LFNQTTGAEP TASIRIQYTP
MLQPITIEGE LVPKAIDELP VIALLCTQAV GTSTIKDAEE LKVKETNRID TTADMLNLLG
FELQPTNDGL IIHPSEFKTN ATVDSLTDHR IGMMLAVASL LSSEPVKIKQ FDAVNVSFPG
FLPKLKLLEN EG
