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MURA_THEYD
ID   MURA_THEYD              Reviewed;         416 AA.
AC   B5YKS2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, 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=THEYE_A1008;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001147; ACI21379.1; -; Genomic_DNA.
DR   RefSeq; WP_012546097.1; NC_011296.1.
DR   RefSeq; YP_002248837.1; NC_011296.1.
DR   AlphaFoldDB; B5YKS2; -.
DR   SMR; B5YKS2; -.
DR   STRING; 289376.THEYE_A1008; -.
DR   EnsemblBacteria; ACI21379; ACI21379; THEYE_A1008.
DR   KEGG; tye:THEYE_A1008; -.
DR   PATRIC; fig|289376.4.peg.989; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_0_0; -.
DR   InParanoid; B5YKS2; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; 537477at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000718; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_1000094729"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         22..23
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         91
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         304
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         326
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         115
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   416 AA;  45238 MW;  BEC7862148C6F028 CRC64;
     MDKLLIFGGL PLKGEVTISG AKNAALPIMA STLLAQGVHI FKRIPKLRDV FTMTELIKRM
     GGIVEFNELC KINTIKINKF EASYDLVKTM RASILVLGPL VARFGRAKVS LPGGCAIGAR
     PVNLHINGLQ KMGAKISLQE GYIIAKASRL MGTKIYFDIP TVTGTENLMM AATLAKGTTI
     IENAAKEPEI VDLANYLILM GAKIEGAGTS IIKVEGVDEL KPPQEYEIIP DRIETGTFIA
     IAGACGGDIS LKGCRIDHID AIILKMKDAG ISFKEIENGI RVIGPKRLQA VDIKTMPYPG
     FPTDMQAQFM AMMTVANGTS VIKETIFENR FMHVAELRRM GADITVEGNT ATIRGVKKLK
     GAPVMATDLR ASASLVIAGL IAEEETLIDR IYHLDRGYEE LDKKLIQLGA RIQRIK
 
 
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