ID   MURA_DESTE              Reviewed;         243 AA.
AC   Q9ZH21;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Flags: Fragment;
GN   Name=murA;
OS   Desulfofundulus thermocisternus (Desulfotomaculum thermocisternum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofundulus.
OX   NCBI_TaxID=42471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 10259 / NBRC 112757 / ST90;
RX   PubMed=10086846; DOI=10.1007/s007920050100;
RA   Larsen O., Lien T., Birkeland N.-K.;
RT   "Dissimilatory sulfite reductase from Archaeoglobus profundus and
RT   Desulfotomaculum thermocisternum: phylogenetic and structural implications
RT   from gene sequences.";
RL   Extremophiles 3:63-70(1999).
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; AF074396; AAC96104.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZH21; -.
DR   SMR; Q9ZH21; -.
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; -; 2.
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..243
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_0000178869"
FT   BINDING         113
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000250|UniProtKB:P0A749"
FT   BINDING         135
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   243 AA;  26491 MW;  408911E43F8AE888 CRC64;
     DLANFLNCLG ARVRGAGTDV IKIEGVDSLG GCLRYAVIPD RIEAGTFMVA AAATRGDVVL
     ENVIPRHLEP LIAKLREAGV EVGEEEDRVR VRASGPLSPI DIKTMPYPGF PTDMQSQMMA
     LLSTVPGTSV IVENIFENRF KVADELKRMG ARIKVEGRLA VVEGVERLQG ACVRATDLRA
     GAALVVAGLM AEGETRIDNV QYIDRGYFNL EQKLRMLGAR IWRAPYDEKT PAQDNAVRKS
     ALI