ID C5D975_GEOSW Unreviewed; 435 AA. AC C5D975; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 86. 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 OrderedLocusNames=GWCH70_3288 {ECO:0000313|EMBL:ACS25928.1}; OS Geobacillus sp. (strain WCH70). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS25928.1}; RN [1] {ECO:0000313|EMBL:ACS25928.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS25928.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Brumm P., Mead D.A., Richardson P.; RT "Complete sequence of chromosome of Geopacillus sp. WCH70."; RL Submitted (JUN-2009) 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|ARBA:ARBA00036669, ECO:0000256|HAMAP- CC Rule:MF_00111}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00111}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000256|ARBA:ARBA00038367, 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; CP001638; ACS25928.1; -; Genomic_DNA. DR AlphaFoldDB; C5D975; -. DR STRING; 471223.GWCH70_3288; -. DR KEGG; gwc:GWCH70_3288; -. DR eggNOG; COG0766; Bacteria. DR HOGENOM; CLU_027387_0_0_9; -. DR OrthoDB; 9803760at2; -. DR UniPathway; UPA00219; -. 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; Enolpyruvate transferase domain; 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 NCBIfam; TIGR01072; murA; 1. DR PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1. DR PANTHER; PTHR43783:SF1; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 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|ARBA:ARBA00022490, 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}. FT DOMAIN 6..407 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT ACT_SITE 117 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 22..23 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 93 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 122..126 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" FT MOD_RES 117 FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" SQ SEQUENCE 435 AA; 46549 MW; D9CBCB6895B29552 CRC64; MEKIIVRGGN RLSGTVKVEG AKNAVLPVIA ATLLASNGKS VIHDVPALSD VYTISEVLRY LGADVKIEEN TITVDASQEL KFEAPFEYVR KMRASVLVMG SLLARNGRAR VALPGGCAIG SRPIDQHLKG FEAMGAHVKV GNGFIDAEVK GRLRGAKIYL DFPSVGATEN IMMAAVLAEG TTIIENCAKE PEIVDLANFL NAMGAKVRGA GTGTIRIEGV DQLTGTTHTV IPDRIEAGTF MVAAAITGGN VLVQGAVPEH LSSLIAKMEE MGVTIIEEGN GLRVIGPEKL KAVDIKTMPY PGFPTDMQSQ MMALLLKAEG TSMVTETVFE NRFMHVEEFR RMNADIKIEG RSVIINGPCN LQGAEVAATD LRAAAALILA GLAAEGYTRV TELRHLDRGY VRFHEKLAAL GADIERVNDE SETAAEDVKV KDLNI //