(data stored in SCRATCH3701 zone)

SWISSPROT: MURA_VIBVY

ID   MURA_VIBVY              Reviewed;         421 AA.
AC   Q7MPA3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 110.
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=VV0461;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
DR   EMBL; BA000037; BAC93225.1; -; Genomic_DNA.
DR   RefSeq; WP_011149386.1; NC_005139.1.
DR   SMR; Q7MPA3; -.
DR   STRING; 672.VV93_v1c04290; -.
DR   PRIDE; Q7MPA3; -.
DR   EnsemblBacteria; BAC93225; BAC93225; BAC93225.
DR   GeneID; 2623228; -.
DR   KEGG; vvy:VV0461; -.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; 537477at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002675; Chromosome I.
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;
DR   PRODOM; Q7MPA3.
DR   SWISS-2DPAGE; Q7MPA3.
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Pyruvate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..421
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_0000178951"
FT   REGION          23..24
FT                   /note="Phosphoenolpyruvate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   REGION          121..125
FT                   /note="UDP-N-acetylglucosamine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   REGION          161..164
FT                   /note="UDP-N-acetylglucosamine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         92
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         306
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         328
FT                   /note="UDP-N-acetylglucosamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   MOD_RES         116
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   421 AA;  44739 MW;  FED1ACEFB6CBF4C2 CRC64;
     MEKFRVIGST QPLMGEVTIS GAKNAALPIL FASILAEEPV EVANVPHLRD IDTTMELLKR
     LGAKVERNGS VHVDPSSIDE YCAPYDLVKT MRASIWALGP LVARFGQGQV SLPGGCAIGA
     RPVDLHITGL EQLGATITLE DGYVKAHVDG RLQGAHIVMD KVSVGATITI MCAATLAEGT
     TVLDNAAREP EIVDTAKFLN TLGAKISGAG TDTITIEGVE RLGGGKHAVV ADRIETGTFL
     VAAAVSGGKV VCHNTQAHLL EAVLAKLEEA GALVETGEDW ISVDMTGREL KAVNIRTAPH
     PGFPTDMQAQ FTLLNMMAKG GGVITETIFE NRFMHVPELK RMGAKAEIEG NTVICGDVER
     LSAAQVMATD LRASASLVIA GCIAKGETIV DRIYHIDRGY DKIENKLNAL GAKIERFRES
     N
//

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