AROA_ACICJ
ID AROA_ACICJ Reviewed; 445 AA.
AC A5FUH8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; OrderedLocusNames=Acry_0031;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00210}.
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; CP000697; ABQ29260.1; -; Genomic_DNA.
DR RefSeq; WP_007424234.1; NC_009484.1.
DR AlphaFoldDB; A5FUH8; -.
DR SMR; A5FUH8; -.
DR STRING; 349163.Acry_0031; -.
DR PRIDE; A5FUH8; -.
DR EnsemblBacteria; ABQ29260; ABQ29260; Acry_0031.
DR KEGG; acr:Acry_0031; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_5; -.
DR OMA; YEDHRMA; -.
DR OrthoDB; 533829at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000000245; 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid 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; -; 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 Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_1000058592"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..102
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 28..29
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 33
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 129
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 353
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 357
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 399
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ SEQUENCE 445 AA; 45982 MW; 16104C7D825F7565 CRC64;
MEHAATLPQT SRRPATPLTG TITVPGDKSI SHRALMFAGL AVGETRISGL LEGEDVLRTA
AAMRALGATV ERTGPGAWRA SGPGIGGLQS PDDVLDMGNS GTAARLLCGI LASHDIFAVM
TGDASLRRRP MRRVIDPLGA TGAVFAAREG GRLPLSVRGA AEAMPLSYRL PVASAQVKSA
LLLAGLNARG ITEIEEPEPT RDHSENMLRH FGAEVEVAAH GTGKLIRLRG QPELRGADVV
VPGDPSSAAF PIVAALIVPG SRVTIGGVGL NPLRTGLFLT LREMGAAIEI VNAREAGGEP
VGDLIVTASD LRAVDVPAER APSMIDEYPI LAVACAMARG SSRLRGLAEL RVKESDRLAA
TLAMITANGV KAQVDGDDLI IEGGGARGGA TVATHMDHRL AMSALVMGLA TETPVTIDDA
RFIDTSFPGF LPLMRGIGAA IEAAA
