ID   A0A4S2DTE2_LACRE        Unreviewed;       425 AA.
AC   A0A4S2DTE2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-NOV-2019, entry version 4.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN   ORFNames=E5338_07920 {ECO:0000313|EMBL:TGY45848.1}, FOD75_01245
GN   {ECO:0000313|EMBL:QDR71831.1};
OS   Lactobacillus reuteri.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1598 {ECO:0000313|EMBL:TGY45848.1};
RN   [1] {ECO:0000313|EMBL:TGY45848.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NM12_1-47 {ECO:0000313|EMBL:TGY45848.1};
RA   Navarre W., Wong E., Huang K., Tropini C., Ng K., Yu B.;
RT   "Microbes associate with the intestines of laboratory mice.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QDR71831.1, ECO:0000313|Proteomes:UP000316394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL7 {ECO:0000313|EMBL:QDR71831.1,
RC   ECO:0000313|Proteomes:UP000316394};
RA   Milovic A., Bassam K., Barbour A.G.;
RT   "Gastrointestinal microbiota of Peromyscus leucopus, the white-footed
RT   mouse.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-
CC         glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483;
CC         EC=2.5.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00111,
CC         ECO:0000256|SAAS:SAAS01124343};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767211}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00111}.
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DR   EMBL; CP041676; QDR71831.1; -; Genomic_DNA.
DR   EMBL; SRYI01000028; TGY45848.1; -; Genomic_DNA.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000316394; Chromosome.
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   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;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767221};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767191};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767246};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767261};
KW   Complete proteome {ECO:0000313|Proteomes:UP000316394};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767234};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767219};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:TGY45848.1}.
FT   DOMAIN        7    406       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   REGION      121    125       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    116    116       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   BINDING      92     92       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     306    306       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     328    328       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
SQ   SEQUENCE   425 AA;  45600 MW;  B64CB100286A72C7 CRC64;
     MKKMIIQGGN RLSGEVTIGG AKNSTVALIP AAILADTPVE FDTVPDILDV HNLMIILESM
     NVKSEFSHGV LDIDPTQIVE AELPSKAIKS LRASYYFMGA LLGRFHRATL TFPGGDNIGP
     RPIDQHLKAF KALGATVSEE KGTVHLDAPN GLHGSRIFLD MVSVGATINA ILAAVRAEGT
     TIIENAAREP EIIDLATFLN NMGAKIRGTG TDTIRITGVK ALQSMNTHTI IADRIEAGTY
     LSLAAALGDG VMIHNVIPEH LESFTSKMIE MGVNLQIDSD KIYVPKSSNL HPVTVKTMPF
     PGFATDLQQP LTPLMSLADG DSTIVDTIYP KRVKHISQLQ KMGMKIEAHD GMIVVKHTEE
     LHGAEVSAGE IRAGAALTIA GLMADGQTVI NNAGNILRGY DRIVWKLNRL HANVSIEDDS
     SVKIG
//