ID   A0A4S2DTE2_LACRE        Unreviewed;       425 AA.
AC   A0A4S2DTE2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   10-FEB-2021, entry version 8.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN   ORFNames=FOD75_01245 {ECO:0000313|EMBL:QDR71831.1};
OS   Lactobacillus reuteri.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1598 {ECO:0000313|EMBL:QDR71831.1, ECO:0000313|Proteomes:UP000316394};
RN   [1] {ECO:0000313|EMBL:QDR71831.1, ECO:0000313|Proteomes:UP000316394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL7 {ECO:0000313|EMBL:QDR71831.1,
RC   ECO:0000313|Proteomes:UP000316394};
RA   Milovic A., Bassam K., Barbour A.G.;
RT   "Gastrointestinal microbiota of Peromyscus leucopus, the white-footed
RT   mouse.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00111};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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DR   EMBL; CP041676; QDR71831.1; -; Genomic_DNA.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000316394; 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: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 {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00111};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00111};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00111, ECO:0000313|EMBL:QDR71831.1}.
FT   REGION          22..23
FT                   /note="Phosphoenolpyruvate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   REGION          121..125
FT                   /note="UDP-N-acetylglucosamine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         92
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         306
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         328
FT                   /note="UDP-N-acetylglucosamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   425 AA;  45600 MW;  B64CB100286A72C7 CRC64;
     MKKMIIQGGN RLSGEVTIGG AKNSTVALIP AAILADTPVE FDTVPDILDV HNLMIILESM
     NVKSEFSHGV LDIDPTQIVE AELPSKAIKS LRASYYFMGA LLGRFHRATL TFPGGDNIGP
     RPIDQHLKAF KALGATVSEE KGTVHLDAPN GLHGSRIFLD MVSVGATINA ILAAVRAEGT
     TIIENAAREP EIIDLATFLN NMGAKIRGTG TDTIRITGVK ALQSMNTHTI IADRIEAGTY
     LSLAAALGDG VMIHNVIPEH LESFTSKMIE MGVNLQIDSD KIYVPKSSNL HPVTVKTMPF
     PGFATDLQQP LTPLMSLADG DSTIVDTIYP KRVKHISQLQ KMGMKIEAHD GMIVVKHTEE
     LHGAEVSAGE IRAGAALTIA GLMADGQTVI NNAGNILRGY DRIVWKLNRL HANVSIEDDS
     SVKIG
//