ID MURA2_STAAN Reviewed; 419 AA. AC P65457; Q99SD4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 122. DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00111}; DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=Enoylpyruvate transferase 2 {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 2 {ECO:0000255|HAMAP-Rule:MF_00111}; DE Short=EPT 2 {ECO:0000255|HAMAP-Rule:MF_00111}; GN Name=murA2 {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ; GN OrderedLocusNames=SA1926; OS Staphylococcus aureus (strain N315). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N315; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=N315; RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.; RT "Shotgun proteomic analysis of total and membrane protein extracts of S. RT aureus strain N315."; RL Submitted (OCT-2007) to UniProtKB. CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- CC acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + phosphate; 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:0000255|HAMAP-Rule:MF_00111}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000255|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; BA000018; BAB43210.1; -; Genomic_DNA. DR PIR; A99906; A99906. DR RefSeq; WP_000046602.1; NC_002745.2. DR AlphaFoldDB; P65457; -. DR SMR; P65457; -. DR EnsemblBacteria; BAB43210; BAB43210; BAB43210. DR KEGG; sau:SA1926; -. DR HOGENOM; CLU_027387_0_0_9; -. DR BioCyc; MetaCyc:MONOMER-15461; -. 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro. DR CDD; cd01555; UdpNAET; 1. DR FunFam; 3.65.10.10:FF:000001; UDP-N-acetylglucosamine 1-carboxyvinyltransferase; 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 NCBIfam; NF006873; PRK09369.1; 1. DR NCBIfam; NF009470; PRK12830.1; 1. DR PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1. DR PANTHER; PTHR43783:SF2; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE 2; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; KW Cytoplasm; Peptidoglycan synthesis; Pyruvate; Transferase. FT CHAIN 1..419 FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2" FT /id="PRO_0000178919" FT ACT_SITE 118 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT BINDING 24..25 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT BINDING 94 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT BINDING 123..127 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT BINDING 307 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT BINDING 329 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT MOD_RES 118 FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" SQ SEQUENCE 419 AA; 45075 MW; 05C1CE1332B060CC CRC64; MAQEVIKIRG GRTLNGEVNI SGAKNSAVAI IPATLLAQGH VKLEGLPQIS DVKTLVSLLE DLNIKASLNG TELEVDTTEI QNAALPNNKV ESLRASYYMM GAMLGRFKKC VIGLPGGCPL GPRPIDQHIK GFKALGAEID ESSTTSMKIE AKELKGAHIF LDMVSVGATI NIMLAAVYAT GQTVIENAAK EPEVVDVANF LTSMGANIKG AGTSTIKING VKELHGSEYQ VIPDRIEAGT YMCIAAACGE NVILNNIVPK HVETLTAKFS ELGVNVDVRD ERIRINNNAP YQFVDIKTLV YPGFATDLQQ PITPLLFMAN GPSFVTDTIY PERFKHVEEL KRMGANIEVD EGTATIKPST LHGAEVYASD LRAGACLIIA GLIAEGVTTI YNVKHIYRGY TDIVEHLKAL GADIWTETV //