(data stored in ACNUC7421 zone)

SWISSPROT: MURA_ANADE

ID   MURA_ANADE              Reviewed;         422 AA.
AC   Q2IMV5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=Adeh_0364;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.
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: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; CP000251; ABC80140.1; -; Genomic_DNA.
DR   RefSeq; WP_011419423.1; NC_007760.1.
DR   SMR; Q2IMV5; -.
DR   STRING; 290397.Adeh_0364; -.
DR   PRIDE; Q2IMV5; -.
DR   EnsemblBacteria; ABC80140; ABC80140; Adeh_0364.
DR   KEGG; ade:Adeh_0364; -.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   BioCyc; ADEH290397:G1G5W-374-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001935; 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   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; 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;
DR   PRODOM; Q2IMV5.
DR   SWISS-2DPAGE; Q2IMV5.
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    422       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase.
FT                                /FTId=PRO_1000023018.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   REGION      124    128       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    119    119       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
FT   BINDING      95     95       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     119    119       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   422 AA;  44494 MW;  0559F37622A07053 CRC64;
     MDKIVIEGGV PLRGSVDVSG AKNAALPVIA AALLAEGEHE VRNVPDLADV RTLGKLLGHM
     GCEVVRGEGD RRTVRLRVPA AVTPEAPYEL VKTMRASVLV LGPLLARLGR ARVSLPGGCA
     IGARPIDQHL KALTALGAEI RLEHGYVNAS VPGGRLRGTV FTFDAQTVTG TENVMMAAAL
     AEGETVLRNC AREPEVKDLG DALVAMGALV EGAGTDEIWI EGVPSLRPLS HAVIPDRIEA
     GTFLVAGALP GNDVTVRGCV AAHQEALVEK LRAVGAEVTK VEGGLRVIGD GRPRPVDVRT
     APHPGFPTDM QAQLMVLLCL ADGTSRITET VFENRFMHVQ ELIRLGAHVE VDGRVAMVKG
     VPELSGAPVM ASDLRASAAL VLAGLAATGT TEVLRVYHLD RGYERIEEKL APLGARIRRV
     RG
//

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