ID A0A2U1K4N7_9BACI Unreviewed; 429 AA.
AC A0A2U1K4N7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:PWA12362.1};
GN ORFNames=DCC39_06045 {ECO:0000313|EMBL:PWA12362.1};
OS Pueribacillus theae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pueribacillus.
OX NCBI_TaxID=2171751 {ECO:0000313|EMBL:PWA12362.1, ECO:0000313|Proteomes:UP000245998};
RN [1] {ECO:0000313|EMBL:PWA12362.1, ECO:0000313|Proteomes:UP000245998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T8 {ECO:0000313|EMBL:PWA12362.1,
RC ECO:0000313|Proteomes:UP000245998};
RA Niu L.;
RT "Camelliibacillus theae gen. nov., sp. nov., isolated from Pu'er tea.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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, 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|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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWA12362.1}.
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; QCZG01000009; PWA12362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1K4N7; -.
DR OrthoDB; 9809920at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000245998; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000245998};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00210}.
FT DOMAIN 9..423
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT REGION 92..95
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 343
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 122
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 342
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 346
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 388
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ SEQUENCE 429 AA; 45821 MW; A3020750A946C977 CRC64;
MGKRLSPANQ PLQGELKVPG DKSISHRSIM LGAVANGTTT IKGFLPGEDC INTIKCFKKL
GVPIEIEKED VIVVGNGFEG LQEPNDVLYV GNSGTLNRLL LGLLAGRPFH SVLYGDESIA
SRPMDRVAKP LRQMGAVIDG RKNGSYPPIS VRGGNLKGIE YESPVASAQV KSAILLAGLQ
ANGVTTITEP ALSRDHTERM LTAFGVELKR ENTTVSLEGN QRLHGTNIQV PADISSAAFF
IVTALITKDS ELTLTDVGMN PTRSGIVDAL LAMGANITML NERQINGEPV ADLHIKSSPL
KNIEINGELI PRLIDEIPIL ALAATQAEGK MVISDAEELK VKETNRIDAV VNQLRLLGAN
IEATEDGMII EGRTNLHGGT VDSLGDHRIG MMLAIASLVA SGEVVLQNEG CISISYPDFF
PDLANLKNN
//
