ID   MURA_METEP              Reviewed;         429 AA.
AC   A9W480;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Mext_1987;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000908; ABY30386.1; -; Genomic_DNA.
DR   RefSeq; WP_012253521.1; NC_010172.1.
DR   AlphaFoldDB; A9W480; -.
DR   SMR; A9W480; -.
DR   STRING; 419610.Mext_1987; -.
DR   EnsemblBacteria; ABY30386; ABY30386; Mext_1987.
DR   KEGG; mex:Mext_1987; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_0_5; -.
DR   OMA; CDPHRAT; -.
DR   BioCyc; MEXT419610:MEXT_RS10055-MON; -.
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_1000094699"
FT   ACT_SITE        126
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         102
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         316
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         338
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         126
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   429 AA;  45150 MW;  BF71A1B5981C6251 CRC64;
     MDRIHITGGT PLNGTIPISG AKNAALPLMI ASLLTGETLE LINVPRLADI AALTRILGNH
     GVDHMVVGKR PGQTAETGQT VRLTASNVID TTAPYELVST MRASFWVIAP LLARFGEAKV
     SLPGGCAIGT RPVNLLIMAL EKLGAEIEID GGYVVAKTKN GLRGAEIVFP SVTVGGTHVA
     LMAAALAYGT TVIDNAAREP EVVDLAECLI KMGARIEGAG TSRIVVEGVA RLGGTRHEVL
     PDRIETGTYA MAVAMTGGDV SLVNTRTDLL ASALETLAST GTEVTALPDG IRVRRNGGGI
     SPADVTTDPF PGFPTDLQAQ FMALMTLAKG QSRIRETIFE NRFMHVQELA RLGARIRLDG
     DLAVVEGVER LKGAPVMATD LRASVSLVIG ALAAEGETQI NRVYHLDRGF EALEAKLARC
     GAQIERVRA