ID A0A4D6GTJ9_HALS9 Unreviewed; 430 AA. AC A0A4D6GTJ9; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 4. 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 ECO:0000313|EMBL:QCC45043.1}; GN ORFNames=HBSAL_06945 {ECO:0000313|EMBL:QCC45043.1}; OS Halobacterium salinarum (strain ATCC 33171 / DSM 3754 / JCM 8978 / OS NBRC 102687 / NCIMB 764 / 91-R6). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; OC Halobacteriales; Halobacteriaceae; Halobacterium. OX NCBI_TaxID=2597657 {ECO:0000313|EMBL:QCC45043.1, ECO:0000313|Proteomes:UP000296216}; RN [1] {ECO:0000313|Proteomes:UP000296216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33171 / DSM 3754 / JCM 8978 / NBRC 102687 / NCIMB 764 / RC 91-R6 {ECO:0000313|Proteomes:UP000296216}; RX PubMed=31296677; DOI=10.1128/MRA.00429-19; RA Pfeiffer F., Marchfelder A., Habermann B., Dyall-Smith M.L.; RT "The genome sequence of the Halobacterium salinarum type strain is RT closely related to that of laboratory strains NRC-1 and R1."; RL Microbiol Resour Announc 8:e00429-e00429(2019). 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 -!- 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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00210}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00210}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00210}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP038631; QCC45043.1; -; Genomic_DNA. DR UniPathway; UPA00053; -. DR Proteomes; UP000296216; Chromosome. 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; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210}; KW Complete proteome {ECO:0000313|Proteomes:UP000296216}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00210, KW ECO:0000313|EMBL:QCC45043.1}. FT DOMAIN 7 421 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT REGION 1 21 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 20 21 Shikimate-3-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00210}. FT REGION 89 92 Phosphoenolpyruvate. {ECO:0000256|HAMAP- FT Rule:MF_00210}. FT REGION 164 166 Shikimate-3-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00210}. FT ACT_SITE 312 312 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00210}. FT ACT_SITE 340 340 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00210}. FT BINDING 25 25 Shikimate-3-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_00210}. FT BINDING 119 119 Phosphoenolpyruvate. {ECO:0000256|HAMAP- FT Rule:MF_00210}. FT BINDING 192 192 Shikimate-3-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_00210}. FT BINDING 339 339 Shikimate-3-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_00210}. FT BINDING 343 343 Phosphoenolpyruvate. {ECO:0000256|HAMAP- FT Rule:MF_00210}. FT BINDING 386 386 Phosphoenolpyruvate. {ECO:0000256|HAMAP- FT Rule:MF_00210}. SQ SEQUENCE 430 AA; 43246 MW; BF54A3E27F8DA6FE CRC64; MHATVSPSRV RGRARAPPSK SYTHRALLAA GYADGETVVR DPLVSADTRA TARAVGLLGG AATRENGDWV VTGFGSRPAV PDAVIDCANS GTTMRLVTAA AALADGTTVL TGDASLRARP HGPLLDTLSG LGGTARSTRG NGQAPLVVDG PVSGGSVALP GDVSSQFVTA LLMAGAVTET GIETDLTTEL KSAPYVDITL DVLDAFGVSA SETAAGYRVP GGQAYAPSGA EYAVPGDFSS ASYLLAAGAL AAADGAAVVV EGMHPSAQGD AAIVDVLDRM GADIDWDTES GVITVQRSEL SGVEVGVADT PDLLPTIAVL GAAADGTTRI TDAEHVRYKE TDRVAAMAES LSKLGASVEE RPDELVVHGG DTELSGASVD GRGDHRLVMA LAVAGLVADG ETTIAGSEHV DVSFPDFFEV LAGLGADADG //