(data stored in ACNUC7421 zone)

SWISSPROT: AROA_RHOPS

ID   AROA_RHOPS              Reviewed;         445 AA.
AC   Q13ER0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 85.
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=RPD_0189;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE37429.1; -; Genomic_DNA.
DR   RefSeq; WP_011500621.1; NC_007958.1.
DR   SMR; Q13ER0; -.
DR   STRING; 316057.RPD_0189; -.
DR   PRIDE; Q13ER0; -.
DR   EnsemblBacteria; ABE37429; ABE37429; RPD_0189.
DR   KEGG; rpd:RPD_0189; -.
DR   eggNOG; ENOG4105CMY; Bacteria.
DR   eggNOG; COG0128; LUCA.
DR   HOGENOM; HOG000247371; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   OrthoDB; 533829at2; -.
DR   BioCyc; RPAL316057:RPD_RS00960-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000001818; 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: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;
DR   PRODOM; Q13ER0.
DR   SWISS-2DPAGE; Q13ER0.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..445
FT                   /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT                   /id="PRO_1000058610"
FT   REGION          28..29
FT                   /note="Shikimate-3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   REGION          99..102
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   ACT_SITE        356
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         33
FT                   /note="Shikimate-3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         129
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         355
FT                   /note="Shikimate-3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         359
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         402
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   445 AA;  46883 MW;  8A5F222CFD54E488 CRC64;
     MSHSDQTSPL EARKSAALSG TARVPGDKSI SHRALILGAL AVGETRISGL LEGQDVIDTG
     KAMRALGARV ERTGEFAWTV RGVGVAGFAQ PEAPLDFGNS GTGCRLAMGA VAGSPITATF
     DGDASLRSRP MRRIVDPLEQ MGARVIQSHE GGRLPLTLQG ARDPLPITYR TPVPSAQIKS
     AVLLAGLSAP GVTTVIEAEA SRDHTELMLQ HFGATLVTEP EGAHGRKISL TGQPELRGAR
     VVVPADPSSA AFPMVAALLV PGSDIVLTEV MTNPLRTGLI TTLREMGGAI EESETRDDTG
     EPMAQFRIRG SRLRGVEVPP ERAPSMIDEY LVLAVAAAFA EGTTVMRGLH ELRVKESDRL
     EATADMLRVN GVKVEIVGDD LIVEGKGHVP GGGLVATHMD HRIAMSALVM GLAADRPVKV
     DDTAFIATSF PDFVPMMRRL GGELA
//

If you have problems or comments...

PBIL Back to PBIL home page