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Database: UniProt
Entry: L1PAT0_9FLAO
LinkDB: L1PAT0_9FLAO
Original site: L1PAT0_9FLAO 
ID   L1PAT0_9FLAO            Unreviewed;       399 AA.
AC   L1PAT0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-FEB-2023, entry version 47.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|ARBA:ARBA00012450};
DE            EC=2.5.1.19 {ECO:0000256|ARBA:ARBA00012450};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|ARBA:ARBA00030046};
GN   ORFNames=HMPREF9075_00240 {ECO:0000313|EMBL:EKY12789.1};
OS   Capnocytophaga sp. oral taxon 332 str. F0381.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1127692 {ECO:0000313|EMBL:EKY12789.1, ECO:0000313|Proteomes:UP000010419};
RN   [1] {ECO:0000313|EMBL:EKY12789.1, ECO:0000313|Proteomes:UP000010419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0381 {ECO:0000313|EMBL:EKY12789.1,
RC   ECO:0000313|Proteomes:UP000010419};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000256|ARBA:ARBA00004811}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|ARBA:ARBA00009948}.
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:EKY12789.1}.
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DR   EMBL; AMET01000015; EKY12789.1; -; Genomic_DNA.
DR   RefSeq; WP_009416006.1; NZ_KB291319.1.
DR   AlphaFoldDB; L1PAT0; -.
DR   STRING; 1127692.HMPREF9075_00240; -.
DR   PATRIC; fig|1127692.3.peg.229; -.
DR   eggNOG; COG0128; Bacteria.
DR   HOGENOM; CLU_024321_0_0_10; -.
DR   OrthoDB; 9809920at2; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000010419; Unassembled WGS sequence.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-EC.
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-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
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   PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   PIRSF; PIRSF000505; EPSPS; 2.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010419};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKY12789.1}.
FT   DOMAIN          54..390
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   COILED          309..336
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   399 AA;  44180 MW;  A86A9E9F31DE597E CRC64;
     MSTLSLLLSG SKSESNRALL LQALFPDMTI GNLAIADDTR IFQKALLNMS PLFDVHHAGT
     AMRFLTAYFA TQRGVDLTLL GSERMCQRPI GVLVEALRAL GADITYTQNE GYPPLRIRGR
     ALKGSQVSLR GDVSSQYASA LLLIAPSLPK GLTLNLTGEI TSLPYLQMTV RFLQYMLGEN
     VAQFVDERTI IVKPCDELLH DHWQVESDWS SASYWYSCVA LSKVGTKLKL SHFKQDSLQG
     DSALQKLYIP LGVHTHFEGT TITIEKVSQP TTTHYRAHLN DTPDIAQTIA VTCLGLGIGA
     TLTGLHTLKI KETDRLQALK NEMEKLQATV HITDDTLQLA PCTELGRGVS ISTYNDHRMA
     MAIAPLLLKT DFQIADKEVV SKSYPNFWDD FAEVMEFCK
//
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