(data stored in ACNUC30630 zone)

SWISSPROT: AROA_TROW8

ID   AROA_TROW8              Reviewed;         443 AA.
AC   Q83I86;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 112.
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=TW194;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(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}.
DR   EMBL; BX251410; CAD66871.1; -; Genomic_DNA.
DR   RefSeq; WP_011096152.1; NC_004551.1.
DR   SMR; Q83I86; -.
DR   PRIDE; Q83I86; -.
DR   EnsemblBacteria; CAD66871; CAD66871; TW194.
DR   GeneID; 29578366; -.
DR   KEGG; tws:TW194; -.
DR   HOGENOM; HOG000247373; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   BioCyc; GCF_000196075:G1EE9-215-MONOMER; -.
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: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; PS00885; EPSP_SYNTHASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q83I86.
DR   SWISS-2DPAGE; Q83I86.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..443
FT                   /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT                   /id="PRO_1000099763"
FT   REGION          25..26
FT                   /note="Shikimate-3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   REGION          115..118
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   REGION          188..190
FT                   /note="Shikimate-3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   ACT_SITE        331
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   ACT_SITE        359
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         30
FT                   /note="Shikimate-3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         145
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         217
FT                   /note="Shikimate-3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         362
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         404
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         428
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   443 AA;  48072 MW;  EE4730740B85E244 CRC64;
     MAKTEMYQPP LGNRALFKMS IPGSKSLTNR HLIIAAIASG ETTIHNLLES RDTNLMIEGL
     RRIGCKIEKL NHTGTHDTGV ISPHCTCLND LIQPSDVRII PSKHYTCSTK IDCGLAGTVM
     RFLPVLAGLC KGSVEFFGDD QAIRRPMDGT LHALRKLGVQ VDGDRIPFTV HGRGEIEGGA
     LETTEHSSSQ FISGLLLSAC RFKNGLTLKH IGNPLPSRPY IDMTVEVMRE WGINVTHSDG
     VWAVTPKELT GKHITIEPDL SNAAPFMIGA IVTGGSATIQ NWPSKTSQPG KYLEAILPQF
     GAEITKTANT ITVSGTGNIT GIRADLGHIG ELVPNLVALA TLAETPSVFY NIGHIRYHET
     DRIEALVNEI SSLGGTITAG KDYIKITPTT LTRSGVWKTY KDHRMATSGA IIGLRHKLTI
     EDIECTSKTF PRFADLWSGA FGK
//

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