ID A0A414E3H3_9FIRM Unreviewed; 430 AA. AC A0A414E3H3; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 14-DEC-2022, entry version 9. 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=DW802_02875 {ECO:0000313|EMBL:RHD24463.1}; OS Ruminococcus bromii. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminococcus. OX NCBI_TaxID=40518 {ECO:0000313|EMBL:RHD24463.1, ECO:0000313|Proteomes:UP000284544}; RN [1] {ECO:0000313|EMBL:RHD24463.1, ECO:0000313|Proteomes:UP000284544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM32-13AC {ECO:0000313|EMBL:RHD24463.1, RC ECO:0000313|Proteomes:UP000284544}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RHD24463.1}. 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; QSIY01000001; RHD24463.1; -; Genomic_DNA. DR AlphaFoldDB; A0A414E3H3; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000284544; 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; EPT/RTPC-like; 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}. FT DOMAIN 6..407 FT /note="EPSP_synthase" 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 307 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 329 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 430 AA; 46109 MW; D88DEDA4E0068359 CRC64; MEKFVVTGGK PLSGEVTISG AKNAAVAIIP AVILCDEPCQ IENIPNISDV SLISRILQQM GANVRRINRS SLYIDPTKIR TCNAVTDLVR GMRASYYLLG ALLGKYGKAK VALPGGCNFG VRPIDQHLKG FEALGATTQL VDGAIIEAEC DRLVGTHVYL DVVSVGATMN IMLAASKAKG QTIIENAARE PHIVDLANFL NSMGADVRGA GTDVIKIRGV EYLHGITYSI IPDQIEAGTY MCAAAATRGC ITVKNITPKH LESISAKLRE MGVKITEYDE ALKVDASSAP LKRCNIKTMP HPGFPTDCQP QFAALLMSVP GTSIINENVW DNRYQYVSEL IRMGAQISVE GRLAIIEGGV PLTAAPVKAT DLRAGAAMII AALEINGTTE ISNIQFIERG YEDVVEKFRG LGADIKKVYF TGDNEQELGA //