ID A0A1L8TJX1_ENTGA Unreviewed; 419 AA. AC A0A1L8TJX1; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 07-APR-2021, entry version 22. 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=murAB {ECO:0000313|EMBL:STD83460.1}; GN Synonyms=murA {ECO:0000256|HAMAP-Rule:MF_00111}; GN ORFNames=EB54_03074 {ECO:0000313|EMBL:RBT37343.1}, GTI89_12535 GN {ECO:0000313|EMBL:MXS26885.1}, NCTC12360_01927 GN {ECO:0000313|EMBL:STD83460.1}; OS Enterococcus gallinarum. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1353 {ECO:0000313|EMBL:STD83460.1, ECO:0000313|Proteomes:UP000254807}; RN [1] {ECO:0000313|EMBL:RBT37343.1, ECO:0000313|Proteomes:UP000252411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=298EA1 {ECO:0000313|EMBL:RBT37343.1, RC ECO:0000313|Proteomes:UP000252411}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Van Tyne D., Lebreton F., Saavedra J.T., Gilmore M.S., RA Manson Mcguire A., Clock S., Crupain M., Rangan U., Young S., RA Abouelleil A., Cao P., Chapman S.B., Griggs A., Priest M., Shea T., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus gallinarum 298EA1."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:STD83460.1, ECO:0000313|Proteomes:UP000254807} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC12360 {ECO:0000313|EMBL:STD83460.1, RC ECO:0000313|Proteomes:UP000254807}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MXS26885.1, ECO:0000313|Proteomes:UP000439965} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E3404 {ECO:0000313|EMBL:MXS26885.1, RC ECO:0000313|Proteomes:UP000439965}; RA Liang G., Bushman F.; RT "Step-wise assembly of the neonatal virome modulated by breast feeding."; 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 -!- 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; WVTI01000012; MXS26885.1; -; Genomic_DNA. DR EMBL; LERZ01000019; RBT37343.1; -; Genomic_DNA. DR EMBL; UFYW01000001; STD83460.1; -; Genomic_DNA. DR RefSeq; WP_003127375.1; NZ_WVTI01000012.1. DR EnsemblBacteria; RBT37343; RBT37343; EB54_03074. DR EnsemblBacteria; STD83460; STD83460; NCTC12360_01927. DR GeneID; 60393829; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000252411; Unassembled WGS sequence. DR Proteomes; UP000254807; Unassembled WGS sequence. DR Proteomes; UP000439965; 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}; Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00111, ECO:0000313|EMBL:STD83460.1}. FT DOMAIN 7..407 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 /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" FT MOD_RES 116 FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" SQ SEQUENCE 419 AA; 44815 MW; 62B5BEF5D4559F59 CRC64; MKKIVIQGNR PLKGEVTISG AKNSAVALIP AAILADSPVV LEGVPDIQDV HSLIEILEIM GVQTHFEENT LTIDPTEIVS IPMPSGKINS LRASYYFMGA LLGKFGEGVV GLPGGCFLGP RPIDLHIKGF EALGATVTNE HGAMYLRTSE AGLAGERIFL DMVSIGATIN VMLAAVKAKG KTIIENAARE PEIIDVATLL NNMGAKIRGA GTNEIRIEGV QELHGCRHSI IPDRIEAGTY LSLAAAAGEG ITIKNVIYEH LESYIAKLEE IGVRMDISED EIYVYPSKDL KPANVKTYPY PGFATDLQQP ITPLLLKANG TSEILDTIYA KRVNHIPELA RMGAQATTEG NLILLNGPSQ LHGAEVVASD LRAGACLVIA GLMATGTTTV FNVEYILRGY DHIIDKLTAL GADIQMVEE //