ID   MURA_WOLWR              Reviewed;         425 AA.
AC   C0R4M1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; OrderedLocusNames=WRi_011710;
OS   Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=66084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wRi;
RX   PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA   Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA   Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA   Andersson S.G.;
RT   "The mosaic genome structure of the Wolbachia wRi strain infecting
RT   Drosophila simulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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 =
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: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}.
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DR   EMBL; CP001391; ACN95863.1; -; Genomic_DNA.
DR   RefSeq; WP_007549225.1; NZ_MKIF01000094.1.
DR   AlphaFoldDB; C0R4M1; -.
DR   SMR; C0R4M1; -.
DR   STRING; 66084.WRi_011710; -.
DR   EnsemblBacteria; ACN95863; ACN95863; WRi_011710.
DR   KEGG; wri:WRi_011710; -.
DR   HOGENOM; CLU_027387_0_0_5; -.
DR   OMA; CRFGQRN; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001293; Chromosome.
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; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Pyruvate; Transferase.
FT   CHAIN           1..425
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_1000119128"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         23..24
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         100
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         313
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         335
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         124
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   425 AA;  45868 MW;  3585C43F9734B76B CRC64;
     MHKILIRNNY KPLVGKIKIN GSKNAVLPIM AASLLSSSPV ILHNVPDLID VHLMSKLLES
     LGAEVNFMHN KNYKANHTLK IDCSNINNHV MPYKTASKLR TSFLILGPML SRFGKARTAF
     PGGCNIGKRP VDMHIKALEE MGAKIEIDGY NIIATVKGKL QGKEITFEKI SVGATENVIM
     AATFAEGVTT INNAATEPEV LDLIDFLKKM GADIEIDNTK VVITGVEALN GCVHKIIPDR
     IEAGTYALAA IITGGKLELE GINLSDIRCI TNELETIGAM VELYDGGIVI SRKNGSIKSA
     NVATDPYPNF PSDMQPQLMS AMCIADGISV IEENIFENRF THADELRKLG ANISIEKSKA
     TISGIKSLSG ANLYATDLRS TAALVLASLV AGGETIINNS HHLWRGYEAM HEKLNSCGAD
     ISISS