ID   MURA1_LACLA             Reviewed;         427 AA.
AC   Q9CI17;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   02-SEP-2026, entry version 147.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT 1 {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA1 {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murA;
GN   OrderedLocusNames=LL0549; ORFNames=L134243;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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 = UDP-
CC         N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + phosphate;
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; AE005176; AAK04647.1; -; Genomic_DNA.
DR   PIR; E86693; E86693.
DR   AlphaFoldDB; Q9CI17; -.
DR   SMR; Q9CI17; -.
DR   EnsemblBacteria; AAK04647; AAK04647; L134243.
DR   KEGG; lla:L134243; -.
DR   PATRIC; fig|272623.7.peg.587; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_0_9; -.
DR   OrthoDB; 9803760at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002196; Chromosome.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01555; UdpNAET; 1.
DR   FunFam; 3.65.10.10:FF:000001; UDP-N-acetylglucosamine 1-carboxyvinyltransferase; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 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   NCBIfam; TIGR01072; murA; 1.
DR   NCBIfam; NF006873; PRK09369.1; 1.
DR   PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR   PANTHER; PTHR43783:SF1; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Pyruvate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..427
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1"
FT                   /id="PRO_0000178879"
FT   ACT_SITE        121
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         24..25
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         97
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         126..130
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         309
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         331
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         121
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   427 AA;  45772 MW;  79EA8B2F476F422E CRC64;
     MMDKIIVKGG QTKLQGEVEI EGAKNAVLPL LAATLLASEG EVVLTNVPIL SDVFMMNNLV
     NHLGTAISFD QEAKKIIAKS NSEIKTTAPY EYVSKMRASI VVMGPILARN GQARVSMPGG
     CSIGSRPIDL HLRGFEQMGA TITQNAGYIE AKADKLKGAH IYLDFPSVGA TQNLILAATL
     ADGTTTLENA AREPEIVDLA NLLNKMGANV KGAGTDTIII KGVEKMHGAN HSVVQDRIEA
     GTFMVAAAMT QGDVLIKDAI AEHNRPLISK LSEMGVNFIQ EESGLRVVGP EKLKATSVKT
     LPHPGFPTDM QSQMTAAQAV AVGESVMVET VFENRFQHLK EMRRIGLEVD ITRNTALIQG
     NSNLQGAAVK STDLRASAAL ILLGLVAKGQ TTVRRLSHLD RGYYKFHEKL KALGADIIRV
     EDEDGEG
//