(data stored in ACNUC7421 zone)

SWISSPROT: AROA_ANADE

ID   AROA_ANADE              Reviewed;         440 AA.
AC   Q2IMC8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 89.
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};
GN   OrderedLocusNames=Adeh_0184;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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-
CC       phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and
CC       inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate;
CC         Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19;
CC         Evidence={ECO:0000255|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: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.
CC       {ECO:0000255|HAMAP-Rule:MF_00210}.
DR   EMBL; CP000251; ABC79961.1; -; Genomic_DNA.
DR   RefSeq; WP_011419244.1; NC_007760.1.
DR   SMR; Q2IMC8; -.
DR   STRING; 290397.Adeh_0184; -.
DR   PRIDE; Q2IMC8; -.
DR   EnsemblBacteria; ABC79961; ABC79961; Adeh_0184.
DR   KEGG; ade:Adeh_0184; -.
DR   eggNOG; ENOG4105CMY; Bacteria.
DR   eggNOG; COG0128; LUCA.
DR   HOGENOM; HOG000247371; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   BioCyc; ADEH290397:G1G5W-190-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000001935; 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; Q2IMC8.
DR   SWISS-2DPAGE; Q2IMC8.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN         1    440       3-phosphoshikimate 1-
FT                                carboxyvinyltransferase.
FT                                /FTId=PRO_0000325329.
FT   REGION       28     29       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   REGION       96     99       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   ACT_SITE    318    318       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   ACT_SITE    346    346       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING      33     33       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     126    126       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     345    345       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     349    349       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     391    391       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   440 AA;  46088 MW;  F30D504DCBF1A062 CRC64;
     MSAAPTSGPL TCRRAGPLRG AIEVPGDKSI SHRSLLFGAL STGETRVTGL LDAEDVHSTR
     KAVEALGAIV REEGGEVVVT PPATLREPGD VIDCGNSGTS LRLLTGVLSG VPGLSVLTGD
     ASLRRRPVRR VIDPLRAMGA NLSARDGDRL PPVVVRGGPL RGARQVLPVA SAQVKSAILL
     AGLFAEGETT VVEPEKSRDH TERMLRGMGV PVKVSGLEVS VSAARPAGGR VDVPGDISSA
     AFFLCGAAAL PGSEVTVRNL GVNETRTGLL DVLRAMGADV WLANLREVAG EPRADVTVRA
     DRLEATEIRG ATIPRLIDEL PVVMVMATQA RGRTVIRDAK ELRVKESDRL AAMGETLARA
     GARIELYEDG CAIEGPTPLR GVEVRTRLDH RIAMSMAVAQ LFCGGEPVVL DDVACVATSF
     PSFFRLLDQV AARVSVGGAP
//

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