(data stored in ACNUC7421 zone)

SWISSPROT: C6B2R0_RHILS

ID   C6B2R0_RHILS            Unreviewed;       420 AA.
AC   C6B2R0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_00210};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210};
GN   OrderedLocusNames=Rleg_0576 {ECO:0000313|EMBL:ACS54880.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54880.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54880.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54880.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC       phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-
CC       phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and
CC       inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00763674}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00830632}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00830582}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00649168}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00210}.
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DR   EMBL; CP001622; ACS54880.1; -; Genomic_DNA.
DR   RefSeq; WP_012756256.1; NC_012850.1.
DR   ProteinModelPortal; C6B2R0; -.
DR   EnsemblBacteria; ACS54880; ACS54880; Rleg_0576.
DR   KEGG; rlg:Rleg_0576; -.
DR   HOGENOM; HOG000247372; -.
DR   KO; K00800; -.
DR   OMA; PSKSMAH; -.
DR   OrthoDB; POG091H02JK; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   Gene3D; 3.65.10.10; -; 3.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
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; 2.
DR   PIRSF; PIRSF000505; EPSPS; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2R0.
DR   SWISS-2DPAGE; C6B2R0.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00830623};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000313|EMBL:ACS54880.1}.
FT   DOMAIN       12    262       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   DOMAIN      287    409       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       26     27       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   REGION       95     98       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   REGION      170    172       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   ACT_SITE    297    297       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   ACT_SITE    325    325       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   BINDING      31     31       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     125    125       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     320    320       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     324    324       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     328    328       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     375    375       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     400    400       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   420 AA;  44360 MW;  8D942530CE8801F6 CRC64;
     MTRTAKLTII PPGRPLSGRA MPPGSKSITN RALLLAGLAK GTSRLTGALK SDDTRYMAEA
     LRAMGVTIDE PDDTTFVVTG SGRLLPPKAP LFLGNAGTAT RFLTAAAALV DGTVIVDGDE
     HMRKRPIGPL VEAMRTLGID VSAETGCPPV TVKGTGRFQA DRIRIDGGLS SQYVSALLMM
     AAGGDRPIDI ELVGEDIGAL GYIDLTTAAM KAFGAKVEKT SPVTWRVEPT GYHAADFIVE
     PDASAATYLW AAEVLTGGAI DLGVPSDAFS QPDARAYDMI AKFPHLPSEI DGSQMQDAVP
     TLAVLAAFNE TPVRFVGIAN LRVKECDRIQ ALSTGLNRIV SGLAREEGDD LIVQSDPALV
     GQHLPAEIDS FADHRIAMSF ALAGLKIDGI TILDPDCVGK TFPAYWRTLA ALGVTYQDKD
//

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