ID E4U9Q2_OCEP5 Unreviewed; 447 AA.
AC E4U9Q2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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};
DE Flags: Precursor;
GN Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210};
GN OrderedLocusNames=Ocepr_1763 {ECO:0000313|EMBL:ADR37216.1};
OS Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 /
OS 506).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Oceanithermus.
OX NCBI_TaxID=670487 {ECO:0000313|EMBL:ADR37216.1, ECO:0000313|Proteomes:UP000008722};
RN [1] {ECO:0000313|Proteomes:UP000008722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC {ECO:0000313|Proteomes:UP000008722};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Zhang X., Brettin T.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Faehnrich R.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of chromosome of Oceanithermus profundus DSM
RT 14977.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR37216.1, ECO:0000313|Proteomes:UP000008722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC {ECO:0000313|Proteomes:UP000008722};
RX PubMed=21677858; DOI=10.4056/sigs.1734292;
RA Pati A., Zhang X., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Hauser L.,
RA Jeffries C.D., Brambilla E.M., Rohl A., Mwirichia R., Rohde M.,
RA Tindall B.J., Sikorski J., Wirth R., Goker M., Woyke T., Detter J.C.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Oceanithermus profundus type strain (506).";
RL Stand. Genomic Sci. 4:210-220(2011).
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; CP002361; ADR37216.1; -; Genomic_DNA.
DR RefSeq; WP_013458386.1; NC_014761.1.
DR AlphaFoldDB; E4U9Q2; -.
DR STRING; 670487.Ocepr_1763; -.
DR KEGG; opr:Ocepr_1763; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_0; -.
DR OrthoDB; 9809920at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000008722; Chromosome.
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:UP000008722};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00210}.
FT DOMAIN 27..437
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT REGION 109..112
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 40..41
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 45
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 140
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 186..188
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 362
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 403
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 428
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ SEQUENCE 447 AA; 46989 MW; 1B1D814A6DCBDD02 CRC64;
MSEADLEARS PWSTLAGVAA VRLAPPPGPV RAELAVPGSK SVTNRAIVLA GLAEGASELA
GILKSDDAWW ALEALRTLGL EVEVMGETAR IAGGGGRWPA GEAEVYIGAA GTLGRFLPPA
LAAAPAGRFR VRASRRMSQR PIAPLVDALR ALGGRVDYAG EEGRFPLVVH GAGLAGGEVT
IPGHVSSQFT SGVLLAAPYA RGPVTVRVAG GMVQPAYVRI TLAMMRAFGA EAEEDAELSE
ISVKPGRYRG QRLELEADAS SAAYFFALAA ASGGEVTVTN IGSATLQPDL GFVHVLERMG
ARVELTPRRT TVRGPEKLRG GFTVSLKAMS DQTPTLAALA ALADAPVTIT EVAHVRHHES
DRIAAMAAEL AKLGLRAEER PDGLTVWPGR PRPARLDPHD DHRIAMALSL LALAAPGLEI
ANPGTTSKTF PRYWDYLERL GFHVETV
//
