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AROA_MYCTO
ID   AROA_MYCTO              Reviewed;         450 AA.
AC   P9WPY4; L0TDI9; P22487;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
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=MT3324;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47667.1; -; Genomic_DNA.
DR   PIR; E70590; E70590.
DR   RefSeq; WP_003416914.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPY4; -.
DR   SMR; P9WPY4; -.
DR   EnsemblBacteria; AAK47667; AAK47667; MT3324.
DR   KEGG; mtc:MT3324; -.
DR   PATRIC; fig|83331.31.peg.3580; -.
DR   HOGENOM; CLU_024321_0_0_11; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000001020; 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   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..450
FT                   /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT                   /id="PRO_0000426871"
FT   REGION          94..97
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   REGION          426..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
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         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         124
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         167..169
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         196
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         385
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         410
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   450 AA;  46426 MW;  27BB86F9412A07D5 CRC64;
     MKTWPAPTAP TPVRATVTVP GSKSQTNRAL VLAALAAAQG RGASTISGAL RSRDTELMLD
     ALQTLGLRVD GVGSELTVSG RIEPGPGARV DCGLAGTVLR FVPPLAALGS VPVTFDGDQQ
     ARGRPIAPLL DALRELGVAV DGTGLPFRVR GNGSLAGGTV AIDASASSQF VSGLLLSAAS
     FTDGLTVQHT GSSLPSAPHI AMTAAMLRQA GVDIDDSTPN RWQVRPGPVA ARRWDIEPDL
     TNAVAFLSAA VVSGGTVRIT GWPRVSVQPA DHILAILRQL NAVVIHADSS LEVRGPTGYD
     GFDVDLRAVG ELTPSVAALA ALASPGSVSR LSGIAHLRGH ETDRLAALST EINRLGGTCR
     ETPDGLVITA TPLRPGIWRA YADHRMAMAG AIIGLRVAGV EVDDIAATTK TLPEFPRLWA
     EMVGPGQGWG YPQPRSGQRA RRATGQGSGG
 
 
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