ID A0A4S2DTE2_LACRE Unreviewed; 425 AA. AC A0A4S2DTE2; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. 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=E5338_07920 {ECO:0000313|EMBL:TGY45848.1}; OS Lactobacillus reuteri. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1598 {ECO:0000313|EMBL:TGY45848.1}; RN [1] {ECO:0000313|EMBL:TGY45848.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NM12_1-47 {ECO:0000313|EMBL:TGY45848.1}; RA Navarre W., Wong E., Huang K., Tropini C., Ng K., Yu B.; RT "Microbes associate with the intestines of laboratory mice."; RL Submitted (APR-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 ECO:0000256|SAAS:SAAS00767217}. CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = CC phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D- CC glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; CC EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111, CC ECO:0000256|SAAS:SAAS01124343}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111, CC ECO:0000256|SAAS:SAAS00767211}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:TGY45848.1}. 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; SRYI01000028; TGY45848.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. 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|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767221}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767191}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767246}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767261}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767234}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767219}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:TGY45848.1}. FT DOMAIN 7 406 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT REGION 22 23 Phosphoenolpyruvate binding. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT REGION 121 125 UDP-N-acetylglucosamine binding. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT ACT_SITE 116 116 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00111}. FT BINDING 92 92 UDP-N-acetylglucosamine. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT BINDING 306 306 UDP-N-acetylglucosamine. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT BINDING 328 328 UDP-N-acetylglucosamine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT 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 //