MURA_GLUDA
ID MURA_GLUDA Reviewed; 420 AA.
AC A9HFN0; B5ZE16;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=GDI1442, Gdia_2142;
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=21304715; DOI=10.4056/sigs.972221;
RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT diazotrophicus PAl 5, suggest a new standard in genome sequence
RT submission.";
RL Stand. Genomic Sci. 2:309-317(2010).
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}.
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DR EMBL; AM889285; CAP55385.1; -; Genomic_DNA.
DR EMBL; CP001189; ACI51900.1; -; Genomic_DNA.
DR RefSeq; WP_012224739.1; NC_011365.1.
DR AlphaFoldDB; A9HFN0; -.
DR SMR; A9HFN0; -.
DR STRING; 272568.GDI1442; -.
DR EnsemblBacteria; ACI51900; ACI51900; Gdia_2142.
DR EnsemblBacteria; CAP55385; CAP55385; GDI1442.
DR KEGG; gdi:GDI1442; -.
DR KEGG; gdj:Gdia_2142; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_5; -.
DR OMA; CDPHRAT; -.
DR OrthoDB; 537477at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000736; Chromosome.
DR Proteomes; UP000001176; 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;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; Peptidoglycan synthesis; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..420
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_1000075972"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 94
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 307
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT BINDING 329
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT MOD_RES 118
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
SQ SEQUENCE 420 AA; 44569 MW; 6E39E6EF7AF545B6 CRC64;
MDRFIIHGGH RLRGDIVIGG AKNAALKLLV AGLLTSERLV LRNVPRIADI TTMRRLLEQH
GVTVEDLEGD GGTLAVGGTI TNTEAPYDIV SQMRASILVL GPLLARCGEA RVSLPGGCAI
GTRPVDMHLK GLEALGAEIS LENGYINARA PRGLVGERII LPFASVGATE NLLMASCLAR
GRTEIINAAR EPEIADLVAC LNGMGARITG TGTGSLAIEG VEALHGTTHR VMPDRIECGT
YACAAGITGG ELRLIGGRAD HLGAVVRALE EAGVEVFQED DALRVRRTGA LRGVDIMTEP
YPGFPTDMQA QFMALLSVAE GASMVTETIF ENRFMHVPEL NRMGARINVH GSSAIIRGVH
SLSGAPVMAT DLRASFSLIL AGLAAHGETI LSRVYHLDRG YEAVEQKLAR CGAQIERVRE
