ID   A0A4S2DTE2_LIMRT        Unreviewed;       425 AA.
AC   A0A4S2DTE2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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}, FOL80_01830
GN   {ECO:0000313|EMBL:NMV62781.1};
OS   Limosilactobacillus reuteri (Lactobacillus reuteri).
OC   Bacteria; Bacillota; 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.
RN   [2] {ECO:0000313|EMBL:NMV62781.1, ECO:0000313|Proteomes:UP000549512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N4 {ECO:0000313|EMBL:NMV62781.1,
RC   ECO:0000313|Proteomes:UP000549512};
RA   An X.;
RT   "Comparative genomics analysis of genetic diversity and habitat
RT   adaptability of Lactobacillus reuteri from different sources.";
RL   Submitted (AUG-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|ARBA:ARBA00036669, ECO:0000256|HAMAP-
CC         Rule:MF_00111};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00111}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|ARBA:ARBA00038367, 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; VTTE01000007; NMV62781.1; -; Genomic_DNA.
DR   EMBL; CP041676; QDR71831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S2DTE2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000316394; Chromosome.
DR   Proteomes; UP000549512; Unassembled WGS sequence.
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; 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   PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR   PANTHER; PTHR43783:SF2; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE 2; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 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|ARBA:ARBA00022490, 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}.
FT   DOMAIN          6..406
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         22..23
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         92
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         121..125
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         306
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00111"
FT   BINDING         328
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
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
//