AROA_SALTI
ID AROA_SALTI Reviewed; 427 AA.
AC P19786;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
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=STY0978, t1956;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=2235501; DOI=10.1093/nar/18.20.6133;
RA Chatfield S., Dougan G., Charles I.G.;
RT "Complete nucleotide sequence of the aroA gene from Salmonella typhi
RT encoding 5-enolpyruvylshikimate 3-phosphate synthase.";
RL Nucleic Acids Res. 18:6133-6133(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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}.
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DR EMBL; X54545; CAA38417.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD05378.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69570.1; -; Genomic_DNA.
DR PIR; S12096; S12096.
DR RefSeq; NP_455465.1; NC_003198.1.
DR RefSeq; WP_000445205.1; NZ_WSUR01000013.1.
DR AlphaFoldDB; P19786; -.
DR SMR; P19786; -.
DR STRING; 220341.16502141; -.
DR EnsemblBacteria; AAO69570; AAO69570; t1956.
DR KEGG; stt:t1956; -.
DR KEGG; sty:STY0978; -.
DR PATRIC; fig|220341.7.peg.987; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_6; -.
DR OMA; YEDHRMA; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
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_0000088285"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 124
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 169..171
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 197
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 336
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 340
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 344
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 386
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 411
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT CONFLICT 254
FT /note="A -> G (in Ref. 1; CAA38417)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="R -> G (in Ref. 1; CAA38417)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="E -> H (in Ref. 1; CAA38417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 46219 MW; 99F0A7096303B30A CRC64;
MESLTLQPIA RVDGAINLPG SKSVSNRALL LAALACGKTV LTNLLDSDDV RHMLNALSAL
GINYTLSADR TRCDITGNGG PLRASGTLEL FLGNAGTAMR PLAAALCLGQ NEIVLTGEPR
MKERPIGHLV DSLRQGGANI DYLEQENYPP LRLRGGFIGG DIEVDGSVSS QFLTALLMTA
PLAPEDTIIR VKGELVSKPY IDITLNLMKT FGVEIANHHY QQFVVKGGQQ YHSPGRYLVE
GDASSASYFL AAGAIKGGTV KVTGIGRKSM QGDIRFADVL EKMGATITWG DDFIACTRGE
LHAIDMDMNH IPDAAMTIAT TALFAKGTTT LRNIYNWRVK ETDRLFAMAT ELRKVGAEVE
EGHDYIRITP PAKLQHADIG TYNDHRMAMC FSLVALSDTP VTILDPKCTA KTFPDYFEQL
ARMSTPA
