(data stored in SCRATCH zone)

SWISSPROT: AROA_ACIF5

ID   AROA_ACIF5              Reviewed;         433 AA.
AC   B5EQ20;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   11-DEC-2019, entry version 69.
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}; OrderedLocusNames=Lferr_1023;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum
OS   ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-2008) 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-phosphate
CC       (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00210};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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. {ECO:0000255|HAMAP-
CC       Rule:MF_00210}.
DR   EMBL; CP001132; ACH83265.1; -; Genomic_DNA.
DR   RefSeq; WP_012536424.1; NC_011206.1.
DR   SMR; B5EQ20; -.
DR   STRING; 380394.Lferr_1023; -.
DR   EnsemblBacteria; ACH83265; ACH83265; Lferr_1023.
DR   KEGG; afe:Lferr_1023; -.
DR   eggNOG; ENOG4105CMY; Bacteria.
DR   eggNOG; COG0128; LUCA.
DR   HOGENOM; HOG000247371; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   BioCyc; AFER380394:G1GCL-1043-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
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; B5EQ20.
DR   SWISS-2DPAGE; B5EQ20.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..433
FT                   /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT                   /id="PRO_1000118774"
FT   REGION          22..23
FT                   /note="Shikimate-3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   REGION          93..96
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   ACT_SITE        314
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   ACT_SITE        342
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         27
FT                   /note="Shikimate-3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         123
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         341
FT                   /note="Shikimate-3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         345
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT   BINDING         386
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   433 AA;  44810 MW;  C2C6F1F7220BFEC8 CRC64;
     MTRYLVRPGS RLAGRFPVPG DKSISHRAVI LGALAEGVTE VEGLLEGADV LATIAAFRSM
     GVQMEGPDKG HLRIHGAGLQ GLRAPVVPLD CGNSGTAMRL LAGVLAGQPF PSTLVGDASL
     QKRPMGRILN PLRAMGAEIA AQDGRAPLHI HGRPLHGIDY ALPVASAQVK SAVLLAGLYA
     DGQTCVTEPA PTRDHSERML QGFGQPVERH GPRACLRGGG RLCGQALQVP GDISSAAFFL
     LGATIAPGSD LTLEGVGINP TRTGIIEILT RMGARIDLTA LREVGGEPVA DIRVRYAPLQ
     GIAIPPRLVP LAIDEFPALF IAAACAKGQT VITGAEELRV KESDRIAVMA GGLRALGATV
     EERVDGAIIS GSALLGGRVD SHGDHRIAMA FAMAALVAQG DMEILDCANV ATSFPSFPAL
     AQQAGLLLEV ASA
//

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