(data stored in ACNUC7421 zone)

SWISSPROT: MURA2_STRPN

ID   MURA2_STRPN             Reviewed;         419 AA.
AC   Q97QW6;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 118.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase 2 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 2 {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT 2 {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA2 {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ;
GN   OrderedLocusNames=SP_1081;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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-glucosamine;
CC         Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7;
CC         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; AE005672; AAK75194.1; -; Genomic_DNA.
DR   PIR; A95125; A95125.
DR   RefSeq; WP_001227083.1; NZ_AKVY01000001.1.
DR   SMR; Q97QW6; -.
DR   STRING; 170187.SP_1081; -.
DR   EnsemblBacteria; AAK75194; AAK75194; SP_1081.
DR   KEGG; spn:SP_1081; -.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; LVPKAMV; -.
DR   BioCyc; SPNE170187:G1FZB-1110-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000585; 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; Q97QW6.
DR   SWISS-2DPAGE; Q97QW6.
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Pyruvate; Transferase.
FT   CHAIN           1..419
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2"
FT                   /id="PRO_0000178931"
FT   REGION          22..23
FT                   /note="Phosphoenolpyruvate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   REGION          121..125
FT                   /note="UDP-N-acetylglucosamine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         92
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         306
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         328
FT                   /note="UDP-N-acetylglucosamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   MOD_RES         116
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   419 AA;  45025 MW;  5717D819B16DF8E3 CRC64;
     MRKIVINGGL PLQGEITISG AKNSVVALIP AIILADDVVT LDCVPDISDV ASLVEIMELM
     GATVKRYDDV LEIDPRGVQN IPMPYGKINS LRASYYFYGS LLGRFGEATV GLPGGCDLGP
     RPIDLHLKAF EAMGATASYE GDNMKLSAKD TGLHGASIYM DTVSVGATIN TMIAAVKANG
     RTIIENAARE PEIIDVATLL NNMGAHIRGA GTNIIIIDGV ERLHGTRHQV IPDRIEAGTY
     ISLAAAVGKG IRINNVLYEH LEGFIAKLEE MGVRMTVSED SIFVEEQSNL KAINIKTAPY
     PGFATDLQQP LTPLLLRANG RGTIVDTIYE KRVNHVFELA KMDADISTTN GHILYTGGRD
     LRGASVKATD LRAGAALVIA GLMAEGKTEI TNIEFILRGY SDIIEKLRNL GADIRLVED
//

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