ID A0A414E3H3_9FIRM Unreviewed; 430 AA. AC A0A414E3H3; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. 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; Clostridiales; Ruminococcaceae; 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 RT 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 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:SAAS01124343}; 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: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 UniPathway; UPA00219; -. DR Proteomes; UP000284544; Unassembled WGS sequence. 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:UP000284544}; 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:RHD24463.1}. FT DOMAIN 6 407 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT REGION 22 23 Phosphoenolpyruvate binding. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT REGION 122 126 UDP-N-acetylglucosamine binding. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT ACT_SITE 117 117 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00111}. FT BINDING 93 93 UDP-N-acetylglucosamine. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT BINDING 307 307 UDP-N-acetylglucosamine. FT {ECO:0000256|HAMAP-Rule:MF_00111}. FT BINDING 329 329 UDP-N-acetylglucosamine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00111}. FT MOD_RES 117 117 2-(S-cysteinyl)pyruvic acid O- FT phosphothioketal. {ECO:0000256|HAMAP- FT 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 //