(data stored in ACNUC7421 zone)

SWISSPROT: MURA_SINFN

ID   MURA_SINFN              Reviewed;         430 AA.
AC   C3MFX0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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};
GN   OrderedLocusNames=NGR_c02220;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-
CC       glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-
CC       D-glucosamine. {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; CP001389; ACP24021.1; -; Genomic_DNA.
DR   RefSeq; WP_012706806.1; NC_012587.1.
DR   RefSeq; YP_002824774.1; NC_012587.1.
DR   ProteinModelPortal; C3MFX0; -.
DR   SMR; C3MFX0; -.
DR   STRING; 394.NGR_c02220; -.
DR   EnsemblBacteria; ACP24021; ACP24021; NGR_c02220.
DR   GeneID; 7790800; -.
DR   KEGG; rhi:NGR_c02220; -.
DR   PATRIC; fig|394.7.peg.3022; -.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; POG091H01PG; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-EC.
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-UniPathway.
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; 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; C3MFX0.
DR   SWISS-2DPAGE; C3MFX0.
KW   Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Peptidoglycan synthesis; Pyruvate; Reference proteome; Transferase.
FT   CHAIN         1    430       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase.
FT                                /FTId=PRO_1000119121.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   REGION      131    135       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   REGION      172    175       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    126    126       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   BINDING     102    102       UDP-N-acetylglucosamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   BINDING     317    317       UDP-N-acetylglucosamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   BINDING     339    339       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   MOD_RES     126    126       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   430 AA;  45423 MW;  2B106C1C9F48BE0D CRC64;
     MDRIRIVGGN QLHGVIPISG AKNAALPLMI ASLLTDDTLT LENVPHLADV EQLIRILGNH
     GADISVNGRR ERQGESYART IHFTSRNIVS TTAPYELVSK MRASFWVIGP LLAREGKARV
     SLPGGCAIGT RPVDLFIEGL TALGANIEID GGYVNATAPE GGLTGGRYVF PKVSVGATHV
     LMMAATLANG TTVIGNAARE PEVADLAKCL NAMGAKITGA GTGTITIEGV RSLSGARHRV
     LPDRIETGTY AMAVAMTGGD VILEDTEASL LDTALEAIRR AGAEISETNS GIRVVRNGAG
     IRPVDIVTDP FPGFPTDLQA QFMGLMTKSS GVSHITETIF ENRFMHVQEL ARLGAKISLS
     GQTAKIEGVG RLKGAPVMAT DLRASVSLVI AGLAAEGETM VSRVYHLDRG FERLEEKLTR
     CGAHVERVSD
//

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