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Database: UniProt
Entry: A0A085VL16_PSESX
LinkDB: A0A085VL16_PSESX
Original site: A0A085VL16_PSESX 
ID   A0A085VL16_PSESX        Unreviewed;       747 AA.
AC   A0A085VL16;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=IV01_09990 {ECO:0000313|EMBL:KFE56129.1};
OS   Pseudomonas syringae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=317 {ECO:0000313|EMBL:KFE56129.1, ECO:0000313|Proteomes:UP000028631};
RN   [1] {ECO:0000313|EMBL:KFE56129.1, ECO:0000313|Proteomes:UP000028631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAW0119 {ECO:0000313|EMBL:KFE56129.1,
RC   ECO:0000313|Proteomes:UP000028631};
RA   Baltrus D.A., Berge O., Morris C.;
RT   "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL   Submitted (JUL-2014) 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:KFE56129.1}.
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DR   EMBL; JPQU01000029; KFE56129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085VL16; -.
DR   PATRIC; fig|317.175.peg.2075; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000028631; 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:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
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   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR   PROSITE; PS51176; PDH_ADH; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KFE56129.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00210}.
FT   DOMAIN          15..303
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   REGION          404..407
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        627
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        655
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         333..334
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         338
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         434
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         654
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         658
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         699
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   747 AA;  79121 MW;  92B32D7E43B8A8CB CRC64;
     MIDVISMKPV EPMIGRLVVV GLGLIGGSFA KGIRESGLCG EVVGVDLDPQ SRKLAVELGV
     VDRCEEDLAT ACRGADVIQL AVPILAMERV LALLATFDLG GTVLTDVGSA KGNVVKAARL
     AFGAMPRHFV PGHPIAGSEQ SGVEASNAQL FKRHKVILTP LPETDPEALA LVDRLWSALG
     ADVEHMEVER HDEVLAATSH LPHLLAFGLV DSLAKRNENL EIFRYAAGGF RDFTRIAGSD
     PVMWHDIFLA NREAVLRTLD TFQTDLDALR EAMVAGDGRQ LLGVFTRARV AREHFGKILA
     RRAYVEPQEI KDLVFIANPG GSVTGRIRVP GDKSISHRSI MLGSLAEGTT EVEGFLEGED
     ALATLQAFRD MGVVIEGPHH GRLTIHGVGL RGLKAPPGAI YLGNSGTSMR LLSGLLAAQD
     FDSILTGDAS LSRRPMNRVA EPLRAMGAVI ETAAEGRPPI TIRGRKTLKG LTYEMPVASA
     QVKSCLLLAG LYAEGVTTVI EPAPTRDHTE RMLRRFGHPV SVDGARVALE SGPGLQAAKI
     EVPADISSAA FFLVAASIAP GSDLLLEGVG INPTRTGIID ILRLMGGDIT LENQREAGGE
     PLADLRVRSA PLKGIEIPAA LVPLAIDEFP VLFIAAACAQ GRTVLRGAEE LRVKESDRIQ
     VMADGLLALG VSVEPTPDGI IIDGSQIGGG VVNAQGDHRV AMAFSIAALR ANAPIQIHDC
     ANVATSFPNF LALCAQVGMR VAQEGQL
//
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