AROA_KLEPN
ID AROA_KLEPN Reviewed; 427 AA.
AC P24497;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2241161};
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, ECO:0000303|PubMed:2241161};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2241161};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2241161};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2241161};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2241161; DOI=10.1016/0003-9861(90)90140-t;
RA Sost D., Amrhein N.;
RT "Substitution of Gly-96 to Ala in the 5-enolpyruvylshikimate-3-phosphate
RT synthase of Klebsiella pneumoniae results in a greatly reduced affinity for
RT the herbicide glyphosate.";
RL Arch. Biochem. Biophys. 282:433-436(1990).
CC -!- FUNCTION: Target of the herbicide glyphosate. Catalyzes the transfer of
CC the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl
CC of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-
CC phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210,
CC ECO:0000269|PubMed:2241161}.
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; Evidence={ECO:0000255|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: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. {ECO:0000255|HAMAP-
CC Rule:MF_00210, ECO:0000305}.
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DR EMBL; X82415; CAA57812.1; -; Genomic_DNA.
DR PIR; S13266; S13266.
DR AlphaFoldDB; P24497; -.
DR SMR; P24497; -.
DR UniPathway; UPA00053; UER00089.
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:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
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; Aromatic amino acid biosynthesis; Cytoplasm;
KW Herbicide resistance; Transferase.
FT CHAIN 1..427
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088262"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 124
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 169..171
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 197
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 336
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 340
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 344
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 386
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 411
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT VARIANT 96
FT /note="G -> A (in strain: K1. DS21; results in a greatly
FT reduced affinity for the herbicide glyphosate)"
FT /evidence="ECO:0000269|PubMed:2241161"
SQ SEQUENCE 427 AA; 46029 MW; 01AF6E750FC710FF CRC64;
MESLTLQPIA RVDGTVNLPG SKSVSNRALL LAALARGTTV LTNLLDSDDV RHMLNALSAL
GVHYVLSSDR TRCEVTGTGG PLQAGSALEL FLGNAGTAMR PLAAALCLGS NDIVLTGEPR
MKERPIGHLV DALRQGGAQI DYLEQENYPP LRLRGGFTGG DVEVDGSVSS QFLTALLMAS
PLAPQDTVIA IKGELVSRPY IDITLHLMKT FGVEVENQAY QRFIVRGNQQ YQSPGDYLVE
GDASSASYFL AAGAIKGGTV KVTGIGRNSV QGDIRFADVL EKMGATVTWG EDYIACTRGE
LNAIDMDMNH IPDAAMTIAT AALFARGTTT LRNIYNWRVK ETDRLFAMAT ELRKVGAEVE
EGEDYIRITP PLTLQFAEIG TYNDHRMAMC FSLVALSDTP VTILDPKCTA KTFPDYFGQL
ARISTLA
