(data stored in SCRATCH zone)

SWISSPROT: D1CDM3_THET1

ID   D1CDM3_THET1            Unreviewed;       439 AA.
AC   D1CDM3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_00210};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210};
GN   OrderedLocusNames=Tter_0107 {ECO:0000313|EMBL:ACZ41029.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41029.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41029.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:
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:0000256|HAMAP-Rule:MF_00210,
CC         ECO:0000256|SAAS:SAAS01118199};
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   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS01089941}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS01089951}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00567303}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00210}.
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DR   EMBL; CP001825; ACZ41029.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0107; -.
DR   EnsemblBacteria; ACZ41029; ACZ41029; Tter_0107.
DR   KEGG; ttr:Tter_0107; -.
DR   eggNOG; ENOG4105CMY; Bacteria.
DR   eggNOG; COG0128; LUCA.
DR   HOGENOM; HOG000247371; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   BioCyc; TTER525904:G1GGS-107-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDM3.
DR   SWISS-2DPAGE; D1CDM3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00423060};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00215611};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS01089931};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00215594, ECO:0000313|EMBL:ACZ41029.1}.
FT   DOMAIN        8    421       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       21     22       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   REGION       91     94       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   ACT_SITE    313    313       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   ACT_SITE    341    341       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   BINDING      26     26       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     121    121       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     340    340       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     344    344       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     386    386       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   439 AA;  47197 MW;  865069F3B6CE14E9 CRC64;
     MDITISPARS VHGNIMPPGD KSISHRAAIF GALAQGTTDI YNYSPARDCQ STLECLLSLG
     TGIRRDGNYI RVEGVGDTGF KEPESILDCG NSGTTMRLLI GALAPMDLYA VLIGDKSLTK
     RPMDRVLKPL GDMGLRYYAR NKDRYPPVSI RGGKIQGIHY QTPVASAQVK SAILLAGLRA
     EGETVVTEPA KSRDHTERML KAMGAQIQSD GTTVRLVASR LSATTFHVPA DPSSAAFILA
     AALIVPESKV TTSNICLNPT RIGFLNVLER MGANIEIHNE RESSGEPIGD IEASTSELNG
     IEIGGTEIPT LIDEIPILAV LATQAKGRTV IRDAEELRIK ETDRISVLCR ALQQMGADIR
     EMRDGFEIHG PCKLKGAKVD PDHDHRIAMA LAVASLIAED KTTILGAECA SISYPNFWDH
     LSSLGVELSG TQSDSKTNV
//

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