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Database: UniProt/SWISS-PROT
Entry: MURA1_STRMU
LinkDB: MURA1_STRMU
Original site: MURA1_STRMU 
ID   MURA1_STRMU             Reviewed;         423 AA.
AC   Q8DT57;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-JUN-2016, entry version 90.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT 1 {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA1 {ECO:0000255|HAMAP-Rule:MF_00111};
GN   OrderedLocusNames=SMU_1525;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59175.1; -; Genomic_DNA.
DR   RefSeq; NP_721869.1; NC_004350.2.
DR   RefSeq; WP_002262937.1; NC_004350.2.
DR   ProteinModelPortal; Q8DT57; -.
DR   STRING; 210007.SMU_1525; -.
DR   EnsemblBacteria; AAN59175; AAN59175; SMU_1525.
DR   GeneID; 1028764; -.
DR   KEGG; smu:SMU_1525; -.
DR   PATRIC; 19665057; VBIStrMut61772_1357.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   KO; K00790; -.
DR   OMA; IRTAPHP; -.
DR   OrthoDB; EOG68M4GK; -.
DR   PhylomeDB; Q8DT57; -.
DR   BioCyc; SMUT210007:GC7Z-1430-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002512; 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; Reference proteome; Transferase.
FT   CHAIN         1    423       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase 1.
FT                                /FTId=PRO_0000231278.
FT   REGION       23     24       Phosphoenolpyruvate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   REGION      125    129       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    120    120       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   BINDING      96     96       UDP-N-acetylglucosamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   BINDING     309    309       UDP-N-acetylglucosamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   BINDING     331    331       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   MOD_RES     120    120       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   423 AA;  45617 MW;  CAD40B6A09D0C017 CRC64;
     MDRIIIEGGN TQLKGEVVIE GAKNAVLPLL AAAILPTEGQ TLLKNVPILS DVFTMNNVVR
     GLNVAVDFDE ERNQILVDAT GDILDVAPYE YVSQMRASIV VLGPILARNG HAKVSMPGGC
     TIGSRPIDLH LKGLEAMGAK IQQTGGDITA TADRLKGANI YMDFPSVGAT QNLMMAATLA
     DGTTIIENAA REPEIVDLAN LLNKMGARVI GAGTETLTII GVDKMHGTDH SVVQDRIEAG
     TFMVAAAMTN GNVLVKNAVW EHNRPLISKL REMGVQVTEE ERGIRVISDV TKLRPVTVKT
     MPHPGFPTDM QAQFTALMAV VKGESTMIET VFENRFQHLE EMRRMGLTSE ILRDTAMIHG
     GEQLQGAQVM STDLRASAAL ILTGMVADGK TTVGKLNHLD RGYYQFHEKL TKLGATISRV
     NGE
//
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