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Database: UniProt/SWISS-PROT
Entry: MURA_SALTI
LinkDB: MURA_SALTI
Original site: MURA_SALTI 
ID   MURA_SALTI              Reviewed;         419 AA.
AC   P65455; Q8XF63;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   06-JUL-2016, entry version 88.
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=STY3486, t3224;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07824.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70760.1; -; Genomic_DNA.
DR   RefSeq; NP_457686.1; NC_003198.1.
DR   RefSeq; WP_000357288.1; NZ_LUHL01000042.1.
DR   ProteinModelPortal; P65455; -.
DR   SMR; P65455; 1-418.
DR   STRING; 220341.STY3486; -.
DR   PRIDE; P65455; -.
DR   EnsemblBacteria; AAO70760; AAO70760; t3224.
DR   EnsemblBacteria; CAD07824; CAD07824; CAD07824.
DR   GeneID; 1249742; -.
DR   KEGG; stt:t3224; -.
DR   KEGG; sty:STY3486; -.
DR   PATRIC; 18545060; VBISalEnt120419_3550.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; IRTAPHP; -.
DR   OrthoDB; EOG68M4GK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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   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;
KW   Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Peptidoglycan synthesis; Pyruvate; Transferase.
FT   CHAIN         1    419       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase.
FT                                /FTId=PRO_0000178911.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   REGION      120    124       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   REGION      160    163       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    115    115       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   BINDING      91     91       UDP-N-acetylglucosamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   BINDING     305    305       UDP-N-acetylglucosamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   BINDING     327    327       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   MOD_RES     115    115       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   419 AA;  44741 MW;  CA147092EC0F61AC CRC64;
     MDKFRVQGPT TLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV DTSMKLLSQL
     GAKVERNGSV HIDASQVNVF CAPYDLVKTM RASIWALGPL VARFGQGQVS LPGGCTIGAR
     PVDLHITGLE QLGATIKLEE GYVKASVEGR LKGAHIVMDK VSVGATVTIM CAATLAEGTT
     IIENAAREPE IVDTANFLVT LGAKIAGQGT DRITIEGVER LGGGVYRVLP DRIETGTFLV
     AAAISRGKIL CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP
     AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGARAEIESN TVICHGVETL
     SGAQVMATDL RASASLVLAG CIAEGTTIVD RIYHIDRGYE RIEDKLRALG ANIERVKGE
//
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