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Database: UniProt
Entry: V8FT17_9BURK
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Original site: V8FT17_9BURK 
ID   V8FT17_9BURK            Unreviewed;       437 AA.
AC   V8FT17;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   13-SEP-2023, entry version 44.
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=V757_12095 {ECO:0000313|EMBL:ETD66848.1};
OS   Pelistega indica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pelistega.
OX   NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD66848.1, ECO:0000313|Proteomes:UP000018766};
RN   [1] {ECO:0000313|EMBL:ETD66848.1, ECO:0000313|Proteomes:UP000018766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-7 {ECO:0000313|EMBL:ETD66848.1,
RC   ECO:0000313|Proteomes:UP000018766};
RA   Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT   "Genomic analysis of Pelistega sp. HM-7.";
RL   Submitted (NOV-2013) 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:ETD66848.1}.
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DR   EMBL; AYSV01000133; ETD66848.1; -; Genomic_DNA.
DR   RefSeq; WP_023953221.1; NZ_CABMIG010000133.1.
DR   AlphaFoldDB; V8FT17; -.
DR   PATRIC; fig|1414851.3.peg.2520; -.
DR   OrthoDB; 9809920at2; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000018766; 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   Reference proteome {ECO:0000313|Proteomes:UP000018766};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00210}.
FT   DOMAIN          10..431
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   REGION          98..101
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         24..25
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         29
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         128
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         175..177
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         207
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         352
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         356
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         398
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         423
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   437 AA;  47821 MW;  55D4C4919567249A CRC64;
     MADDYLDLNQ VNQAKGEVTL PGSKSISNRV LLLAALAEGK TRLTGVLKSD DTDVMLAALK
     TLGVRIVQLN HDEYEVEGIN AFDHSQFPQT KADIFLGNAG TAFRPLTAAL AVMGGDYYLH
     GVPRMHERPI KDLVETLQSI GCNIEYKLND GYPPLQINTS NLNVSAPIEI EGSVSSQFLT
     ALLLVSPLIT RKTQQDIQIK VKGELISKPY IAITLNLMER FGVKVENNNW SHFIVAKDAK
     YQAISHLAVE GDASSASYFM ALGLVGGGPI RINGVGKSSI QGDIKFADVL VHMGADIQLQ
     DNSIEVRGHK GLLKAFDMDF NLIPDAAMTA AVLALYADGP CTLRNIASWR VKETDRIEAM
     HKELEKLGAI VSSGSDWLRI EPPKHWRTAS IDTYDDHRMA MCFSLAVFGP VGVRIMDPNC
     VAKTFPTYFD VYKGLVA
//
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