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Database: UniProt/TrEMBL
Entry: H2IHM2_9VIBR
LinkDB: H2IHM2_9VIBR
Original site: H2IHM2_9VIBR 
ID   H2IHM2_9VIBR            Unreviewed;       426 AA.
AC   H2IHM2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   07-JAN-2015, entry version 19.
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   ORFNames=VEJY3_04740 {ECO:0000313|EMBL:AEX21444.1};
OS   Vibrio sp. EJY3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1116375 {ECO:0000313|EMBL:AEX21444.1, ECO:0000313|Proteomes:UP000006799};
RN   [1] {ECO:0000313|EMBL:AEX21444.1, ECO:0000313|Proteomes:UP000006799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EJY3 {ECO:0000313|EMBL:AEX21444.1};
RX   PubMed=22535948; DOI=10.1128/JB.00303-12;
RA   Roh H., Yun E.J., Lee S., Ko H.J., Kim S., Kim B.Y., Song H.,
RA   Lim K.I., Kim K.H., Choi I.G.;
RT   "Genome Sequence of Vibrio sp. Strain EJY3, an Agarolytic Marine
RT   Bacterium Metabolizing 3,6-Anhydro-L-Galactose as a Sole Carbon
RT   Source.";
RL   J. Bacteriol. 194:2773-2774(2012).
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:SAAS00166497}.
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:SAAS00013785}.
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:SAAS00013815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00013766}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|RuleBase:RU004164}.
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DR   EMBL; CP003241; AEX21444.1; -; Genomic_DNA.
DR   RefSeq; YP_005022420.1; NC_016613.1.
DR   EnsemblBacteria; AEX21444; AEX21444; VEJY3_04740.
DR   GeneID; 11665359; -.
DR   KEGG; vej:VEJY3_04740; -.
DR   KO; K00800; -.
DR   BioCyc; VSP1116375:GJV8-991-MONOMER; -.
DR   Proteomes; UP000006799; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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; PS00104; EPSP_SYNTHASE_1; 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:UP000006799};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00013796};
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       94     97       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    314    314       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   ACT_SITE    342    342       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     124    124       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     198    198       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       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     345    345       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     387    387       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     412    412       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   426 AA;  46075 MW;  21E21F5F63ED190A CRC64;
     MESLTLQPIN KIQGEVNLPG SKSVSNRALL LAALAKGTTR LTNLLDSDDI RHMLNALTTL
     GVQYQLSEDK TECVVEGLGQ PFSVSEPVEL FLGNAGTAMR PLAAALCLGE GEYVLTGEPR
     MKERPIGHLV TALQDAGADI EYLENENYPP LKIVGTGLKS GTVSIDGSIS SQFLTAFLMS
     APLAEGEVRI NIEGDLVSKP YIDITLHIMK QFGVNVINND YQEFVIPAGQ HYVAPGDFLV
     EGDASSASYF LAAAAIKGGE VKVTGIGKNS IQGDIQFADA LEKMGAEIEW GDDYVIARAG
     KLKGIDMDYN HIPDAAMTIA TTALFAEGTT AIRNVYNWRV KETDRLSAMA TELRKVGAEV
     EEGEDYIIVK PVPQLKHAAI DTYDDHRMAM CFSLVALSDT PVTINDPKCT SKTFPDYFDK
     LKSLSC
//
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