ID A0A4S2DTE2_LIMRT Unreviewed; 425 AA. AC A0A4S2DTE2; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 03-AUG-2022, entry version 12. 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; 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. 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|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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VTTE01000007; NMV62781.1; -; Genomic_DNA. DR EMBL; CP041676; QDR71831.1; -; Genomic_DNA. DR EnsemblBacteria; TGY45848; TGY45848; E5338_07920. 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; -; 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}. FT DOMAIN 7..406 FT /note="EPSP_synthase" FT /evidence="ECO:0000259|Pfam:PF00275" 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 /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 //