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 01-MAY-2013, entry version 56.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase;
DE EC=2.5.1.19;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase;
DE Short=EPSP synthase;
DE Short=EPSPS;
GN Name=aroA; 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 -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 6/7.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
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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; SNAGPFL; -.
DR ProtClustDB; PRK02427; -.
DR BioCyc; MVAN350058:GIWR-1780-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:HAMAP.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP.
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; RNA3'_cycl/enolpyr_transf_A/B; 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; Transferase.
FT CHAIN 1 446 3-phosphoshikimate 1-
FT carboxyvinyltransferase.
FT /FTId=PRO_1000099729.
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
//
