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Database: UniProt
Entry: A1T5Z3
LinkDB: A1T5Z3
Original site: A1T5Z3 
ID   AROA_MYCVP              Reviewed;         446 AA.
AC   A1T5Z3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   26-NOV-2014, entry version 64.
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=Mvan_1771;
OS   Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-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: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {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}.
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DR   EMBL; CP000511; ABM12593.1; -; Genomic_DNA.
DR   RefSeq; YP_952599.1; NC_008726.1.
DR   ProteinModelPortal; A1T5Z3; -.
DR   SMR; A1T5Z3; 1-428.
DR   STRING; 350058.Mvan_1771; -.
DR   EnsemblBacteria; ABM12593; ABM12593; Mvan_1771.
DR   GeneID; 4647067; -.
DR   KEGG; mva:Mvan_1771; -.
DR   PATRIC; 18181775; VBIMycVan31953_1817.
DR   eggNOG; COG0128; -.
DR   HOGENOM; HOG000247373; -.
DR   KO; K00800; -.
DR   OMA; SYDDHRM; -.
DR   OrthoDB; EOG6Z6FZ4; -.
DR   BioCyc; MVAN350058:GIWR-1780-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; Aromatic amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN         1    446       3-phosphoshikimate 1-
FT                                carboxyvinyltransferase.
FT                                /FTId=PRO_1000099729.
FT   REGION       23     24       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   REGION       98    101       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   REGION      171    173       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   ACT_SITE    315    315       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   ACT_SITE    345    345       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING      28     28       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     128    128       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     200    200       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     348    348       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     389    389       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     414    414       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   446 AA;  45498 MW;  F8AA5380D085C48B CRC64;
     MSTWPAPSTA TPVHATVTVP GSKSQTNRAL VLAALAVPQG SSTISGALRS RDTDLMISAL
     QGLGVVVEAP DTDGSDGTEL TVSGALAPKA GARIDCGLAG TVLRFVPPVA ALTTETVTFD
     GDEQARARPI APLLDGLRAL GVAIDGDGLP FSVRGQGSVR GGTVEIDASG SSQFVSGLLL
     SGAAFTEGLT VVHTGGAVPS APHIAMTVSM LRDAGVEVDD SAADRWRVAP GPIAARHWAV
     EPDLSNAVPF LAAAVISGGT VRVTGWPTVS TQPAATILSL LTSLGSEVRQ GNSHLEVQGA
     TSYDGIDVDL RDVGELAPSV AAMAALASPG SVSRLRGIAH LRGHETDRLA ALSAELNRLG
     GQCEETDDGL VITARQMHGG VWRSYADHRM ATAGAIVGLR VPGVEVEDIG TTAKTLPDFP
     QLWADMLAGQ TDLQAGAPHA GRNQGR
//
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