AROA_STRPN
ID AROA_STRPN Reviewed; 427 AA.
AC Q9S400;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
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, ECO:0000269|PubMed:10601870};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:10601870};
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=SP_1371;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND MASS SPECTROMETRY.
RC STRAIN=NCIMB 40794 / 0100993;
RX PubMed=10601870; DOI=10.1046/j.1432-1327.2000.00994.x;
RA Du W., Wallis N.G., Mazzulla M.J., Chalker A.F., Zhang L., Liu W.-S.,
RA Kallender H., Payne D.J.;
RT "Characterization of Streptococcus pneumoniae 5-enolpyruvylshikimate 3-
RT phosphate synthase and its activation by univalent cations.";
RL Eur. J. Biochem. 267:222-227(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND SHIKIMATE-3-PHOSPHATE ANALOG, FUNCTION, ACTIVE
RP SITE, AND SUBUNIT.
RX PubMed=14763973; DOI=10.1046/j.1365-2958.2003.03885.x;
RA Park H., Hilsenbeck J.L., Kim H.J., Shuttleworth W.A., Park Y.H.,
RA Evans J.N., Kang C.;
RT "Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded
RT state, tetrahedral intermediate-bound state and S3P-GLP-bound state.";
RL Mol. Microbiol. 51:963-971(2004).
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 ECO:0000269|PubMed:10601870, ECO:0000269|PubMed:14763973}.
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, ECO:0000269|PubMed:10601870};
CC -!- ACTIVITY REGULATION: Competitively inhibited by glyphosate. Activated
CC by ammonium, rubidium or potassium ions. {ECO:0000269|PubMed:10601870}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for PEP (with 100 mM ammonium at pH 7 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:10601870};
CC KM=31 uM for S3P (with 100 mM ammonium at pH 7 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:10601870};
CC KM=91 uM for PEP (with 10 mM ammonium at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10601870};
CC KM=100 uM for PEP (with 1 mM ammonium at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10601870};
CC KM=118 uM for S3P (with 10 mM ammonium at pH 7 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:10601870};
CC KM=145 uM for S3P (with 1 mM ammonium at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10601870};
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, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14763973}.
CC -!- INTERACTION:
CC Q9S400; Q97QS2: eno; NbExp=2; IntAct=EBI-2207276, EBI-2207206;
CC Q9S400; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207276, EBI-2207053;
CC Q9S400; Q97NV3: groES; NbExp=2; IntAct=EBI-2207276, EBI-2206949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- MASS SPECTROMETRY: Mass=45825; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10601870};
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00210, ECO:0000305}.
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DR EMBL; AF169483; AAD45819.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75469.1; -; Genomic_DNA.
DR PIR; D95159; D95159.
DR RefSeq; WP_001808726.1; NZ_AKVY01000001.1.
DR PDB; 1RF4; X-ray; 2.20 A; A/B/C/D=1-427.
DR PDB; 1RF5; X-ray; 2.30 A; A/B/C/D=1-427.
DR PDB; 1RF6; X-ray; 1.90 A; A/B/C/D=1-427.
DR PDBsum; 1RF4; -.
DR PDBsum; 1RF5; -.
DR PDBsum; 1RF6; -.
DR AlphaFoldDB; Q9S400; -.
DR SMR; Q9S400; -.
DR IntAct; Q9S400; 3.
DR STRING; 170187.SP_1371; -.
DR DrugBank; DB04539; Glyphosate.
DR DrugBank; DB04328; Shikimate-3-Phosphate.
DR EnsemblBacteria; AAK75469; AAK75469; SP_1371.
DR KEGG; spn:SP_1371; -.
DR eggNOG; COG0128; Bacteria.
DR OMA; YEDHRMA; -.
DR PhylomeDB; Q9S400; -.
DR BioCyc; SPNE170187:G1FZB-1380-MON; -.
DR BRENDA; 2.5.1.19; 1960.
DR SABIO-RK; Q9S400; -.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; Q9S400; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Direct protein sequencing; Transferase.
FT CHAIN 1..427
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088304"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000305|PubMed:14763973"
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 ECO:0000269|PubMed:14763973"
FT BINDING 25
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:14763973"
FT BINDING 90..93
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
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 ECO:0000269|PubMed:14763973"
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 13
FT /note="S -> I (in Ref. 1; AAD45819)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="I -> V (in Ref. 1; AAD45819)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="K -> Q (in Ref. 1; AAD45819)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="G -> C (in Ref. 1; AAD45819)"
FT /evidence="ECO:0000305"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1RF5"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1RF6"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:1RF6"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:1RF6"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1RF6"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1RF5"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:1RF6"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1RF6"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:1RF6"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:1RF6"
SQ SEQUENCE 427 AA; 45766 MW; 45CE6F4D0D1C7B70 CRC64;
MKLKTNIRHL HGSIRVPGDK SISHRSIIFG SLAEGETKVY DILRGEDVLS TMQVFRDLGV
EIEDKDGVIT IQGVGMAGLK APQNALNMGN SGTSIRLISG VLAGADFEVE MFGDDSLSKR
PMDRVTLPLK KMGVSISGQT ERDLPPLRLK GTKNLRPIHY ELPIASAQVK SALMFAALQA
KGESVIIEKE YTRNHTEDML KQFGGHLSVD GKKITVQGPQ KLTGQKVVVP GDISSAAFWL
VAGLIAPNSR LVLQNVGINE TRTGIIDVIR AMGGKLEITE IDPVAKSATL IVESSDLKGT
EIGGALIPRL IDELPIIALL ATQAQGVTVI KDAEELKVKE TDRIQVVADA LNSMGADITP
TADGMIIKGK SALHGARVNT FGDHRIGMMT AIAALLVADG EVELDRAEAI NTSYPSFFDD
LESLIHG
