ID   MURA_VARPS              Reviewed;         429 AA.
AC   C5CQI8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; OrderedLocusNames=Vapar_1163;
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S110;
RX   PubMed=21183664; DOI=10.1128/jb.00925-10;
RA   Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA   O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA   Ovchinnikova G., Goodwin L., Han C.;
RT   "Complete genome sequence of the metabolically versatile plant growth-
RT   promoting endophyte, Variovorax paradoxus S110.";
RL   J. Bacteriol. 193:1183-1190(2011).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00111};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00111}.
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; CP001635; ACS17814.1; -; Genomic_DNA.
DR   RefSeq; WP_012746312.1; NC_012791.1.
DR   AlphaFoldDB; C5CQI8; -.
DR   SMR; C5CQI8; -.
DR   STRING; 543728.Vapar_1163; -.
DR   EnsemblBacteria; ACS17814; ACS17814; Vapar_1163.
DR   GeneID; 45055467; -.
DR   KEGG; vap:Vapar_1163; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_0_4; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; 537477at2; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00111; MurA; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Pyruvate; Transferase.
FT   CHAIN           1..429
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_1000202937"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         22..23
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         93
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         122..126
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         313
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         335
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   MOD_RES         117
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   429 AA;  45608 MW;  1DECB4C187005D2A CRC64;
     MDKLLIRGGR QLRGEVLISG AKNAALPELC AALLTDQPVT LHNVPRLQDV STMLKLVRNM
     GVAAERDDNG TVRLDAGDLS IPEAPYELVK TMRASVLALG PLLARFGHAK VSLPGGCAIG
     SRPVDQHIKG LQAMGAEIVV EHGYMIASLP AGRTRLKGAR ILTDMVTVTG TENFLMAAAL
     AEGETLLENA AQEPEIVDLA EMLIRMGARI EGHGTSHIRI QGVEKLHGCE HAVVADRIEA
     GTFLCAVAAT GGDVFLRHAR ADHMDAVIDK LRDAGCTVAA QEGGVRISSS APACEHLKAQ
     SFSTTEYPGF PTDMQAQFMA LNVIARGASM VTETIFENRF MHVNEMVRLG ATIHVEGKVA
     MVEGVQQLSG ATVMATDLRA SASLVIAGLV ADGETLVDRI YHLDRGYDRM EAKLRGLGAD
     IERISGAAA