ID A0A1L8TJX1_ENTGA Unreviewed; 419 AA. AC A0A1L8TJX1; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 05-JUL-2017, entry version 5. 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=BH745_13305 {ECO:0000313|EMBL:OQO77533.1}, RV03_GL002882 GN {ECO:0000313|EMBL:OJG44384.1}; OS Enterococcus gallinarum. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1353 {ECO:0000313|EMBL:OJG44384.1, ECO:0000313|Proteomes:UP000183081}; RN [1] {ECO:0000313|EMBL:OJG44384.1, ECO:0000313|Proteomes:UP000183081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24841 {ECO:0000313|EMBL:OJG44384.1, RC ECO:0000313|Proteomes:UP000183081}; RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.; RT "Draft genome sequences of 29 type strains of Enterococci."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OQO77533.1, ECO:0000313|Proteomes:UP000192613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1213F 228 {ECO:0000313|EMBL:OQO77533.1, RC ECO:0000313|Proteomes:UP000192613}; RX PubMed=28270110; DOI=.1186/s12866-017-0962-1; RA Beukers A.G., Zaheer R., Goji N., Amoako K.K., Chaves A.V., Ward M.P., RA McAllister T.A.; RT "Comparative genomics of Enterococcus spp. isolated from bovine RT feces."; RL BMC Microbiol. 17:52-52(2017). 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: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D- CC glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha- CC D-glucosamine. {ECO:0000256|HAMAP-Rule:MF_00111, CC ECO:0000256|SAAS:SAAS00767208}. 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:OJG44384.1}. 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; JXKP01000054; OJG44384.1; -; Genomic_DNA. DR EMBL; MJED01000014; OQO77533.1; -; Genomic_DNA. DR RefSeq; WP_003127375.1; NZ_MJED01000014.1. DR UniPathway; UPA00219; -. DR Proteomes; UP000183081; Unassembled WGS sequence. DR Proteomes; UP000192613; 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-HAMAP. 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-HAMAP. 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; 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 Complete proteome {ECO:0000313|Proteomes:UP000183081, KW ECO:0000313|Proteomes:UP000192613}; 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 Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:OJG44384.1}. FT DOMAIN 7 407 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}. FT MOD_RES 116 116 2-(S-cysteinyl)pyruvic acid O- FT phosphothioketal. {ECO:0000256|HAMAP- FT 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 //