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-DEC-2018, entry version 14. 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=C2L98_09555 {ECO:0000313|EMBL:PNY31480.1}, EB54_03074 GN {ECO:0000313|EMBL:RBT37343.1}, 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:PNY31480.1, ECO:0000313|Proteomes:UP000236237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EG1 {ECO:0000313|EMBL:PNY31480.1, RC ECO:0000313|Proteomes:UP000236237}; RA Hiltensperger M., Kumar V., Zegarra-Ruiz D., Dehner C., Khan N., RA Costa F., Tiniakou E., Greiling T., Ruff W., Barbieri A., Kriegel C., RA Jain D., Goodman A.L.; RT "Translocation of a Gut Pathobiont Drives Autoimmunity in Mice and RT Humans."; RL Science 0:0-0(2018). RN [3] {ECO:0000313|EMBL:PNY31480.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EG1 {ECO:0000313|EMBL:PNY31480.1}; RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {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. 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: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 --------------------------------------------------------------------------- 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; PPHK01000006; PNY31480.1; -; Genomic_DNA. DR EMBL; LERZ01000019; RBT37343.1; -; Genomic_DNA. DR EMBL; UFYW01000001; STD83460.1; -; Genomic_DNA. DR RefSeq; WP_003127375.1; NZ_UFYW01000001.1. DR UniPathway; UPA00219; -. DR Proteomes; UP000236237; Unassembled WGS sequence. DR Proteomes; UP000252411; Unassembled WGS sequence. DR Proteomes; UP000254807; 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|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:UP000236237, KW ECO:0000313|Proteomes:UP000252411, ECO:0000313|Proteomes:UP000254807}; 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:STD83460.1}. 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 //