ID A0A2M7B544_9BACT Unreviewed; 421 AA. AC A0A2M7B544; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 11-DEC-2019, entry version 7. 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 ECO:0000313|EMBL:PIU98237.1}; GN ORFNames=COS61_02520 {ECO:0000313|EMBL:PIU98237.1}; OS Candidatus Wolfebacteria bacterium CG03_land_8_20_14_0_80_40_12. OC Bacteria; Candidatus Wolfebacteria. OX NCBI_TaxID=1975069 {ECO:0000313|EMBL:PIU98237.1, ECO:0000313|Proteomes:UP000228949}; RN [1] {ECO:0000313|Proteomes:UP000228949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.K., RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M., RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.; RT "Depth-based differentiation of microbial function through sediment-hosted RT aquifers and enrichment of novel symbionts in the deep terrestrial RT subsurface."; RL Submitted (SEP-2017) 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-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 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 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:PIU98237.1}. 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; PEVJ01000062; PIU98237.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000228949; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767234}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767219}; Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00111, KW ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:PIU98237.1}. FT DOMAIN 7..409 FT /note="EPSP_synthase" FT /evidence="ECO:0000259|Pfam:PF00275" FT REGION 22..23 FT /note="Phosphoenolpyruvate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT ACT_SITE 117 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 93 FT /note="UDP-N-acetylglucosamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 308 FT /note="UDP-N-acetylglucosamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00111" FT BINDING 330 FT /note="UDP-N-acetylglucosamine; via carbonyl oxygen" 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 421 AA; 45964 MW; D2D0BE4FF9A95310 CRC64; MAKFIIQGRK PLKGEIKVAG SKNAALKIFP VSLLTKETIR LSNTPEIEDV FRAGEIVTSL GGEVKKIKPG VFXXXFKNRR RSALPQDLVS KFRASIMFVG PMLAVDGEAE FPHPGGCVIG AGVRPIDMFL DGFKKMGAEI KILDNHYRLT AKKLKGTDIF FPKITVTGTE SLMMTAVLAQ GATILKNCAM EPEIARLADF LNSLGAKIEG AGGPTIKIKG VKKLGAGECR IMPDRIEAGT FAMLAAASNS GEVVIKNAEP NHLEALWVLL DKIGANYVLY KDRIKISPAK KLFTCDVTTH EYPGFATDLQ SPYAVLMTQA EGSSLIHETI YDRRLLFADL LSQMGANVVL CDPHRIVVSG PTKLYGRKLV SPDLRAGISL VMAALISDGK TEIDNIYQID RGYERLDERL RQLGADIKRV D //