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Entry: A0A1H8KYX7_9ACTN
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ID   A0A1H8KYX7_9ACTN        Unreviewed;       411 AA.
AC   A0A1H8KYX7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ORFNames=SAMN05216267_1014157 {ECO:0000313|EMBL:SEN98095.1};
OS   Actinacidiphila rubida.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310780 {ECO:0000313|EMBL:SEN98095.1, ECO:0000313|Proteomes:UP000181951};
RN   [1] {ECO:0000313|EMBL:SEN98095.1, ECO:0000313|Proteomes:UP000181951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEN98095.1,
RC   ECO:0000313|Proteomes:UP000181951};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FODD01000014; SEN98095.1; -; Genomic_DNA.
DR   RefSeq; WP_075017009.1; NZ_FODD01000014.1.
DR   AlphaFoldDB; A0A1H8KYX7; -.
DR   STRING; 310780.SAMN05216267_1014157; -.
DR   OrthoDB; 9809920at2; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000181951; 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; 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.
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:UP000181951};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00210}.
FT   DOMAIN          3..400
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   REGION          79..82
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        296
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        324
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         10..11
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         15
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         109
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         155..157
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         319
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         323
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         327
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         368
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         393
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   411 AA;  43617 MW;  25AF2420C4174C80 CRC64;
     MSVVAVPGSK SVTARALFLA AAAEGTTVLR RPLLSDDTDG FAEGLTRLGY DVRRDADVWL
     ITGRPEGPAA AEADVYCRDA ATAARFLPAL AAAGHGTYRF DASAQMRRRP VAPLTRALRS
     LGVDLTHGEA EGHLPLTVVA DGIKGGEIEL DASLSSQFLT ALLLTGPLTA EGLRIRVTGI
     VSVPYVEITL AMMRRFGVTV ARDGDTFAVP PGGYRATDYA IEPDASTASY FFAAAALTGR
     TATVPGLGAD ALQGDLRFVD VLRRMGAEVE TGPDATTVTG TGRLSGLTVA MRDISDTMPT
     LAAIAPFADG PVRIEDVYNT RVKECDRLEA CAENLRRQGI TVETGHDWIE IRPGTPKPVE
     IACHGDHRIA MSFAVAGLRT PGTTFDDPGC VKKTFPGFHE FFARVRADWG V
//
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