ID A3WBH2_9SPHN Unreviewed; 438 AA.
AC A3WBH2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 95.
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=NAP1_06740 {ECO:0000313|EMBL:EAQ30454.1};
OS Erythrobacter sp. NAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ30454.1, ECO:0000313|Proteomes:UP000002995};
RN [1] {ECO:0000313|EMBL:EAQ30454.1, ECO:0000313|Proteomes:UP000002995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ30454.1,
RC ECO:0000313|Proteomes:UP000002995};
RX PubMed=21952547; DOI=10.1128/JB.05845-11;
RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA Falkowski P.G.;
RT "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT sp. Strain NAP1.";
RL J. Bacteriol. 193:5881-5882(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}.
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:EAQ30454.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAMW01000001; EAQ30454.1; -; Genomic_DNA.
DR RefSeq; WP_007164484.1; NZ_CH672390.1.
DR AlphaFoldDB; A3WBH2; -.
DR STRING; 237727.NAP1_06740; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_5; -.
DR OrthoDB; 9809920at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000002995; 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:UP000002995};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00210}.
FT DOMAIN 8..432
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT REGION 93..96
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 348
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 123
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 347
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 351
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"
SQ SEQUENCE 438 AA; 45697 MW; 55CB38900B885637 CRC64;
MGSYTFTSSA PLKGRLRVPG DKSISHRALM FAGLAVGESR IAGLLEGEDV LATAAAMRQL
GARIVREDDG TWRVNGAGLG SLIEPRAALD MGNSGTSTRL MMGLLASHGL TATFIGDASL
SGRPMNRVIE PLSQMGASFE ASAGGTLPCM LRGASPAVPV TYRLPVASAQ VKSAVLLAGL
NTPGITRVIE PIATRDHTER MLRGFGANLE VSEENGERVI AIHGEADLKP MDVTVPGDPS
SAAFFLVAAS IVPGSDLVVE NVGLNPTRAG IVTVLKQMGA DIKELDPREV GGEPVADLRV
RHAPLKGIEV DPAIVPSMVD EFPVLFVAAA MAEGTTTTTG LEELRVKESD RISVMAAALT
AAGARVEEHE DGLTIHGTGG EPLRGTSNAR VKTHLDHRIA MSMAVAGLAS RDGVEIDDTD
PIATSFPTFM QMLESAAQ
//
