ID   MURA_MYCSM              Reviewed;         104 AA.
AC   Q59561;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase;
DE            EC=2.5.1.7;
DE   AltName: Full=Enoylpyruvate transferase;
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase;
DE            Short=EPT;
DE   Flags: Fragment;
GN   Name=murA;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19420 / DSM 43756 / JCM 5866 / KCTC 9108 / NCTC 8159 / NRRL
RC   B-14616 / Cornell 3;
RX   PubMed=8598279; DOI=10.1111/j.1574-6968.1996.tb07968.x;
RA   Gonzalez-y-Merchand J.A., Estrada-Garcia I., Colston M.J., Cox R.A.;
RT   "A novel method for the isolation of mycobacterial DNA.";
RL   FEMS Microbiol. Lett. 135:71-77(1996).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X87943; CAA61195.1; -; Genomic_DNA.
DR   PIR; S57429; S57429.
DR   AlphaFoldDB; Q59561; -.
DR   SMR; Q59561; -.
DR   STRING; 710686.Mycsm_04708; -.
DR   eggNOG; COG0766; Bacteria.
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-EC.
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-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.65.10.10; -; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Transferase.
FT   CHAIN           <1..104
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_0000178897"
FT   BINDING         13
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:P0A749"
FT   NON_TER         1
SQ   SEQUENCE   104 AA;  11191 MW;  230305A3488B4B07 CRC64;
     AIADGTSMIT ENVFEARFRF VEEMIRLGAD ARTDGHHAVV RGIPQLSSAP VWSSDIRAGA
     GLVLAGLVAD GETEVHDVFH IDRGYPLFVE NLVSLGAEIE RVSS