GenomeNet

Database: UniProt/TrEMBL
Entry: F2NGB6_DESAR
LinkDB: F2NGB6_DESAR
Original site: F2NGB6_DESAR 
ID   F2NGB6_DESAR            Unreviewed;       432 AA.
AC   F2NGB6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   22-JUL-2015, entry version 30.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|RuleBase:RU000531};
DE            EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|RuleBase:RU000531};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210};
GN   OrderedLocusNames=Desac_0647 {ECO:0000313|EMBL:AEB08529.1};
OS   Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Desulfobacca.
OX   NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB08529.1, ECO:0000313|Proteomes:UP000000483};
RN   [1] {ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL   Submitted (MAR-2011) 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-
CC       phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and
CC       inorganic phosphate. {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00240586}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|RuleBase:RU000531,
CC       ECO:0000256|SAAS:SAAS00215600}.
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       ECO:0000256|RuleBase:RU000531}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00240607}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00240595}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|RuleBase:RU004164}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002629; AEB08529.1; -; Genomic_DNA.
DR   ProteinModelPortal; F2NGB6; -.
DR   STRING; 880072.Desac_0647; -.
DR   EnsemblBacteria; AEB08529; AEB08529; Desac_0647.
DR   KEGG; dao:Desac_0647; -.
DR   PATRIC; 54438388; VBIDesAce170587_0707.
DR   KO; K00800; -.
DR   OMA; VIDCANS; -.
DR   BioCyc; DACE880072:GHK9-658-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000000483; 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   Gene3D; 3.65.10.10; -; 2.
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; 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;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|RuleBase:RU000531};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|RuleBase:RU000531};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000483};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00240560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000483};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|RuleBase:RU000531}.
FT   REGION       22     23       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   REGION       91     94       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   REGION      167    169       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   ACT_SITE    310    310       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   ACT_SITE    338    338       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   BINDING      27     27       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     121    121       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     195    195       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     337    337       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     341    341       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     382    382       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     407    407       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   432 AA;  46309 MW;  564CA4A8D8D14B18 CRC64;
     MIYKEIQPVK AMEAVITLPG SKSFSHRALI AAGLARGSSS LRNLLRADDT LMTARALEQL
     GVRITWQEKE CLLEGAGGRL KVPTEPIYLG DSGTSMRFLT AVAALGNGRY VLTGSPRLCQ
     RPIQDLLDAL TLLGVVAHCE NHNGCPPVII QARGLAGGES RVSGGISSQF LSALLLISPF
     AARDVEIEVV GELVSRPYVD ITLSVMEAFG IAYYRRGYQN FCVPAGQRYQ ARDYEVEGDA
     SSASYFLGAA ALTGGRITLT NLNPQSCQGD IGFLEVLQQM GCQVEPTGSG VVLRGRQLQA
     IRINMAHMPD LVPTLAVLAA YAQGETVITG VPHLRHKESD RLQAVATELA KMGITVNQTK
     DGLIIQGGKP RGVVIETYND HRIAMSFALA GLKTPGVMIA NPDCVAKSFP DFWDYFAKLG
     TNSALSASKE NS
//
DBGET integrated database retrieval system