(data stored in ACNUC1104 zone)

SWISSPROT: AROA1_STRCO

ID   AROA1_STRCO             Reviewed;         438 AA.
AC   Q9K4A7;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAY-2019, entry version 108.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00210};
DE            Short=EPSPS 1 {ECO:0000255|HAMAP-Rule:MF_00210};
GN   Name=aroA1 {ECO:0000255|HAMAP-Rule:MF_00210}; Synonyms=aroA2;
GN   OrderedLocusNames=SCO5212; ORFNames=SC7E4.09c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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, ECO:0000305}.
DR   EMBL; AL939122; CAB94597.1; -; Genomic_DNA.
DR   RefSeq; NP_629359.1; NC_003888.3.
DR   RefSeq; WP_003973760.1; NC_003888.3.
DR   SMR; Q9K4A7; -.
DR   STRING; 100226.SCO5212; -.
DR   PRIDE; Q9K4A7; -.
DR   EnsemblBacteria; CAB94597; CAB94597; CAB94597.
DR   GeneID; 1100653; -.
DR   KEGG; sco:SCO5212; -.
DR   PATRIC; fig|100226.15.peg.5296; -.
DR   eggNOG; ENOG4105CMY; Bacteria.
DR   eggNOG; COG0128; LUCA.
DR   HOGENOM; HOG000247373; -.
DR   InParanoid; Q9K4A7; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   PhylomeDB; Q9K4A7; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
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; Q9K4A7.
DR   SWISS-2DPAGE; Q9K4A7.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN         1    438       3-phosphoshikimate 1-
FT                                carboxyvinyltransferase 1.
FT                                /FTId=PRO_0000088302.
FT   REGION       30     31       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   REGION      102    105       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   REGION      178    180       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   ACT_SITE    326    326       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   ACT_SITE    354    354       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING      35     35       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     132    132       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     207    207       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     357    357       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     398    398       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     423    423       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   438 AA;  45851 MW;  8373B568E6C5C353 CRC64;
     MTVNPTHTAL WPAPHASGAV DATVHVPGSK SVTNRALVLA ALASEPGWLR RPLRSRDTLL
     MAEALRTLGV EIEEGVGPEG TGEFWRVIPA GLRGPATVDV GNAGTVMRFL PPVATLADGA
     VRFDGDPRSY ERPLHGVIDA LRVLGARIDD DGRGALPLTV HGGGALEGGP VEIDASSSSQ
     FVSALLLSGP RFNQGVEVRH TGSALPSMPH IRMTVDMLRA VGAQVDTPES GGEPNVWRVT
     PGALLGRDLT VEPDLSNAQP FLAAALVTGG KVVIPDWPSR TTQPGDRLRE IFTDMGGSCE
     LTDFGLVFTG SGAIHGIDVD LSEVGELTPG IAAVAALADS PSTLRGVAHL RLHETDRLAA
     LTKEINELGG DVTETADGLH IRPRRLHGGV FHTYDDHRMA TAGAVLGLAV EGVQIENVAT
     TAKTLPDFPD LWTGMLGA
//

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