ID A0A4D6GTJ9_HALS9 Unreviewed; 430 AA. AC A0A4D6GTJ9; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 13-SEP-2023, entry version 17. 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=APQ99_01712 {ECO:0000313|EMBL:TYO76155.1}, HBSAL_06945 GN {ECO:0000313|EMBL:QCC45043.1}; OS Halobacterium salinarum (strain ATCC 33171 / DSM 3754 / JCM 8978 / NBRC OS 102687 / NCIMB 764 / 91-R6). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=2597657 {ECO:0000313|EMBL:QCC45043.1, ECO:0000313|Proteomes:UP000296216}; RN [1] {ECO:0000313|EMBL:QCC45043.1, ECO:0000313|Proteomes:UP000296216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91-R6 {ECO:0000313|EMBL:QCC45043.1}, and ATCC 33171 / DSM 3754 RC / JCM 8978 / NBRC 102687 / NCIMB 764 / 91-R6 RC {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 Closely RT Related to That of Laboratory Strains NRC-1 and R1."; RL Microbiol. Resour. Announc. 8:e00429-19(2019). RN [2] {ECO:0000313|EMBL:TYO76155.1, ECO:0000313|Proteomes:UP000323075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3754 {ECO:0000313|EMBL:TYO76155.1, RC ECO:0000313|Proteomes:UP000323075}; RA Goeker M.; RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II RT (KMG-II): from individual species to whole genera."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QCC45043.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=91-R6 {ECO:0000313|EMBL:QCC45043.1}; RX PubMed=31797576; RA Pfeiffer F., Losensky G., Marchfelder A., Habermann B., Dyall-Smith M.; RT "Whole-genome comparison between the type strain of Halobacterium salinarum RT (DSM 3754(T)) and the laboratory strains R1 and NRC-1."; RL MicrobiologyOpen 9:0-0(0). CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate CC (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00210}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1- CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, CC ChEBI:CHEBI:145989; EC=2.5.1.19; CC Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|HAMAP- CC Rule:MF_00210}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 6/7. {ECO:0000256|ARBA:ARBA00004811}. 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|ARBA:ARBA00009948, ECO:0000256|HAMAP-Rule:MF_00210}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 EMBL; VRYN01000003; TYO76155.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4D6GTJ9; -. DR EnsemblBacteria; QCC45043; QCC45043; HBSAL_06945. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000296216; Chromosome. DR Proteomes; UP000323075; Unassembled WGS sequence. 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. 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; Enolpyruvate transferase domain; 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 NCBIfam; TIGR01356; aroA; 1. DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1. DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00210}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_00210}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00210}. FT DOMAIN 7..421 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..92 FT /note="Phosphoenolpyruvate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT ACT_SITE 312 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT ACT_SITE 340 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 20..21 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 25 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 119 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 164..166 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 192 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 339 FT /ligand="3-phosphoshikimate" FT /ligand_id="ChEBI:CHEBI:145989" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 343 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210" FT BINDING 386 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000256|HAMAP-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 //