ID E1R955_SPISS Unreviewed; 430 AA.
AC E1R955;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase;
DE EC=2.5.1.19;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase;
GN Name=aroA; OrderedLocusNames=Spirs_3939;
OS Spirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228).
OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX NCBI_TaxID=573413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228;
RX DOI=10.4056/sigs.1143106;
RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Tice H., Cheng J., Pitluck S.,
RA Liolios K., Ivanova N., Tapia R., Han C., Bruce D., Goodwin L.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA Jeffries C., Detter J., Rohde M., Brambilla E., Spring S., Goker M.,
RA Sikorski J., Woyke T., Bristow J., Eisen J., Markowitz V.,
RA Hugenholtz P., Klenk H., Kyrpides N.;
RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT 4228).";
RL Stand. Genomic Sci. 3:136-144(2010).
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; CP002116; ADK83024.1; -; Genomic_DNA.
DR RefSeq; YP_003805618.1; NC_014364.1.
DR ProteinModelPortal; E1R955; -.
DR EnsemblBacteria; ADK83024; ADK83024; Spirs_3939.
DR GeneID; 9492065; -.
DR KEGG; ssm:Spirs_3939; -.
DR PATRIC; 42531996; VBISpiSma89994_4031.
DR HOGENOM; HOG000247372; -.
DR KO; K00800; -.
DR OMA; QYVSALM; -.
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; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Cytoplasm; Transferase.
SQ SEQUENCE 430 AA; 45245 MW; B020BFEBF30E4948 CRC64;
MLVQSNAMKR IVSPGRISGS LKIPGSKSHT IRALLIASAA QGRSIIQDPL DSSDTRAALS
LCRSLGARVT EEQGRWIVEG TGGAMNQAHI DVGNSGTSLF LAAAVAAASD KAVSFDGDEQ
IRRRSAAPLL DALRGLGAEI IESGEAGCAP FTVKGPLQGG KVSIACPTSQ YLSALLLAAP
LTPSGSSTEI EVSLLYERPY VEMTLKWLDD QGIEYQRRGL EWFLVPGGQH YKPFSAAVPA
DFSSATFFFC AAAITGDKLF LKGLDPTDIQ GDKMVLPILE KMGCRVSPKD GGIEIQGPEE
GLSGGTFDLN SIPDALPALA ATACFAKGET QLTNVPQARI KETDRIAVMA QELTGIGAEI
RELEDGLLIS GRGPKGLSGG NVRGHGDHRV IMAEAIAALG AREEVIIDDD GAVAVTFPNF
FSLLDSIRKV
//
