ID   MURA1_STAHJ             Reviewed;         423 AA.
AC   Q4L805;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1;
DE            EC=2.5.1.7;
DE   AltName: Full=Enoylpyruvate transferase 1;
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 1;
DE            Short=EPT 1;
GN   Name=murA1; Synonyms=murZ; OrderedLocusNames=SH0911;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-D-
CC       glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-
CC       glucosamine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
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DR   EMBL; AP006716; BAE04220.1; -; Genomic_DNA.
DR   RefSeq; YP_252826.1; -.
DR   GeneID; 3482039; -.
DR   GenomeReviews; AP006716_GR; SH0911.
DR   KEGG; sha:SH0911; -.
DR   NMPDR; fig|279808.3.peg.1263; -.
DR   HOGENOM; Q4L805; -.
DR   OMA; Q4L805; DNVIPTH.
DR   BioCyc; SHAE279808:SH0911-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltrans...; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA: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   HAMAP; MF_00111; -; 1.
DR   InterPro; IPR001986; EPSP_synthase_core.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Gene3D; G3DSA:3.65.10.10; EPSP_synthase; 2.
DR   PANTHER; PTHR21090:SF4; AcGlu_Tran_MurA; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   ProDom; PD001867; EPSP_synth; 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; Transferase.
FT   CHAIN         1    423       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase 1.
FT                                /FTId=PRO_0000231268.
FT   ACT_SITE    118    118       Proton donor (By similarity).
FT   BINDING     118    118       Phosphoenolpyruvate (covalent) (By
FT                                similarity).
SQ   SEQUENCE   423 AA;  45331 MW;  A8610C691C466CC8 CRC64;
     MTQEVIKIRG GQTLKGDVTI SGAKNSAVAI IPATLLAQGQ VKLDGLPQIS DVETLVSLLE
     DLNIKAHLNG KTLEVDTSEI ENAPLPNNKV ESLRASYYMM GAMLGRFKKC VIGLPGGCPL
     GPRPIDQHIK GFKALGAEID ESNDTSMKIE AKELHGANIF LDMVSVGATI NIMLAAVHAT
     GQTVIENAAK EPEVVDVANF LNSLGADIKG AGTSTLKING VDSLHGSEYQ IIPDRIEAGT
     YMCIAAAVGE EITINNIVPK HVEALTVKLK ELGVDIQVDG DAEKAIIKRK SSYKNVDIKT
     LVYPGFATDL QQPITPLLFM ADGPSFVTET IYPARFRHVD ELKNMGANIE ADMETGTATI
     KPSSLNGAEV YASDLRAGAC LIIAGLLAEG VTTIYNVRHI YRGYTDIVKH LKELGANIWT
     EEV
//