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Database: UniProt
Entry: C0E139_9CORY
LinkDB: C0E139_9CORY
Original site: C0E139_9CORY 
ID   C0E139_9CORY            Unreviewed;       378 AA.
AC   C0E139;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
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   Name=aroA {ECO:0000313|EMBL:EEG27837.1};
GN   ORFNames=CORMATOL_00689 {ECO:0000313|EMBL:EEG27837.1};
OS   Corynebacterium matruchotii ATCC 33806.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=566549 {ECO:0000313|EMBL:EEG27837.1, ECO:0000313|Proteomes:UP000006247};
RN   [1] {ECO:0000313|EMBL:EEG27837.1, ECO:0000313|Proteomes:UP000006247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33806 {ECO:0000313|EMBL:EEG27837.1,
RC   ECO:0000313|Proteomes:UP000006247};
RA   Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA   Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) 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:EEG27837.1}.
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DR   EMBL; ACEB01000006; EEG27837.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0E139; -.
DR   HOGENOM; CLU_024321_0_0_11; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000006247; 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   CDD; cd01556; EPSP_synthase; 1.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEG27837.1}.
FT   DOMAIN          1..366
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
SQ   SEQUENCE   378 AA;  39454 MW;  EC7EA5A1BF2FDD1A CRC64;
     MAQALKRIGV DVQAEPDPDS PANATIFVEP TGFTGGTVDC GLAGTVMRFV PPLAALADGD
     VFFDGDEHAR QRPMKGILDG LRALGISVQG DSLPFKVSGN GSPMGGMVEI NASASSQFVS
     GLLLAAPRFA QGITVRHIGE TLPSMPHIEM TVHMLRQAGA SVDTTTAYQW SVTPGPIRGG
     VVRVEPDLSN ATPFLAAAAV TGSTVQVKDW PTTTTQPGDA IRNILERMGC TVSLTDSDLT
     VTGPKPGSLQ GIEIDMSDIG ELTPTVAAMA TIAKSPSTLT GIAHLHGHET DRLQALATEI
     TKIGGQCSEL PDGLAIKPSG SLHGAHWSTY DDHRMATTGA IIGLVAPGIK VENIETTAKT
     LPGFDRMWAD MVQEMGMP
//
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