AROA_ZYMMO
ID AROA_ZYMMO Reviewed; 453 AA.
AC Q5NLJ0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=ZMO1796;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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}.
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DR EMBL; AE008692; AAV90420.1; -; Genomic_DNA.
DR RefSeq; WP_011241530.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NLJ0; -.
DR SMR; Q5NLJ0; -.
DR STRING; 264203.ZMO1796; -.
DR EnsemblBacteria; AAV90420; AAV90420; ZMO1796.
DR GeneID; 58027499; -.
DR KEGG; zmo:ZMO1796; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_5; -.
DR OMA; YEDHRMA; -.
DR OrthoDB; 533829at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000001173; 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..453
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_1000058620"
FT REGION 99..102
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
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 405
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ SEQUENCE 453 AA; 47788 MW; 5EC83B62C48C3A1C CRC64;
MTRPVHACPL VSRKAPPLSG KVHVPGDKSI SHRALMLSAL AVGESFVEGL LEGEDVLATA
EAMRSMGADI RKDEKGCWHI HGVGVGSLLQ PQNALDMGNS GTSTRLLMGV VASHPITATF
IGDASLSKRP MGRISTPLSL MGARFSAAEG NRLPMTVTGL YPAIPIEYRL PVASAQVKSA
ILLAGLNTPG ITRVIEPVPT RDHSERMLKG YGANLSVEEN DGVRIISIHG EAELKPQHII
VPGDPSSAAF LVVAGLIVPG SDLIVENVGL NPTRSGLYTM LKAMGGQIEY LNPREVGGEP
VADLSVKYSH LKAIDVPPSI VPSMIDEFPI LFIAAAMAEG KSTLQGLAEL RVKESDRIAV
MAEGLKALGV SLEEKEDGLI IEGSAGEGLG QKGKMVSIAA HLDHRIAMSF AVAGLVSEGG
VTIDDRRPIM TSFPVFGQLF KELGAEFEMG LVK
