(data stored in SCRATCH zone)

SWISSPROT: MURA_CHLAB

ID   MURA_CHLAB              Reviewed;         444 AA.
AC   Q5L6U5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 89.
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}; OrderedLocusNames=CAB168;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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; CR848038; CAH63626.1; -; Genomic_DNA.
DR   RefSeq; WP_011096874.1; NC_004552.2.
DR   SMR; Q5L6U5; -.
DR   STRING; 218497.CAB168; -.
DR   EnsemblBacteria; CAH63626; CAH63626; CAB168.
DR   KEGG; cab:CAB168; -.
DR   eggNOG; ENOG4105CDF; Bacteria.
DR   eggNOG; COG0766; LUCA.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; 537477at2; -.
DR   BioCyc; CABO218497:G1GI1-184-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001012; 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; Q5L6U5.
DR   SWISS-2DPAGE; Q5L6U5.
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Peptidoglycan synthesis; Transferase.
FT   CHAIN           1..444
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_0000231188"
FT   REGION          22..23
FT                   /note="Phosphoenolpyruvate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         94
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         309
FT                   /note="UDP-N-acetylglucosamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         331
FT                   /note="UDP-N-acetylglucosamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ   SEQUENCE   444 AA;  48146 MW;  0FE19BB72C13FBB5 CRC64;
     MAAAEVFGGC VLEGSVRVSG AKNSTTKLLV ASLLSDRKCV LRNVPDIGDV RLTVELCRSL
     GSIVHWDKQA EVIEIHTPEI HMSEVSAQFS RVNRIPILLL GALLARCPEG VVVPCVGGDA
     IGERTLNFHF EGLEQLGAKV AYDGHGYQAA APKGLIGAYI TLPYPSVGAT ENLILASVRA
     QGRTIIKNAA LEVEILDLIL FLQKAGVEIT TDNDRTIEIF GCEDFYEVDH WVIPDKIEAA
     SFGMAAVLTG GRVFVENAEQ HLMIPFLKTL RSIGGGFSVT ETGIEFFYNE PLKGGVVLET
     DVHPGFLTDW QQPFSVLLSQ AEGSSVIHET VHENRLGYLR GLQKMGANCE LFYQCLSSKA
     CRYATGNFPH SAIIHGVTPL KASQLVIPDL RAGFAYIMAA LIAEGGPSLI KNTQLLDRGY
     YNWVDKLNSL GAKIHLLSLD PVAF
//

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