MURA_ECOLI
ID MURA_ECOLI Reviewed; 419 AA.
AC P0A749; P28909; Q2M923;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
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}; Synonyms=murZ;
GN OrderedLocusNames=b3189, JW3156;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=K12 / AB1157;
RX PubMed=1512209; DOI=10.1128/jb.174.17.5748-5752.1992;
RA Marquardt J.L., Siegele D.A., Kolter R., Walsh C.T.;
RT "Cloning and sequencing of Escherichia coli murZ and purification of its
RT product, a UDP-N-acetylglucosamine enolpyruvyl transferase.";
RL J. Bacteriol. 174:5748-5752(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O26 / NGY47;
RX PubMed=10103182; DOI=10.1128/aac.43.4.789;
RA Horii T., Kimura T., Sato K., Shibayama K., Ohta M.;
RT "Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing
RT Escherichia coli O26.";
RL Antimicrob. Agents Chemother. 43:789-793(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21445328; DOI=10.1371/journal.pbio.1001033;
RA Mutschler H., Gebhardt M., Shoeman R.L., Meinhart A.;
RT "A novel mechanism of programmed cell death in bacteria by toxin-antitoxin
RT systems corrupts peptidoglycan synthesis.";
RL PLoS Biol. 9:E1001033-E1001033(2011).
RN [6] {ECO:0007744|PDB:1UAE}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYLGLUCOSAMINE AND FOSFOMYCIN, AND ACTIVE SITE.
RX PubMed=8994972; DOI=10.1016/s0969-2126(96)00153-0;
RA Skarzynski T., Mistry A., Wonacott A., Hutchinson S.E., Kelly V.A.,
RA Duncan K.;
RT "Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme
RT essential for the synthesis of bacterial peptidoglycan, complexed with
RT substrate UDP-N-acetylglucosamine and the drug fosfomycin.";
RL Structure 4:1465-1474(1996).
RN [7] {ECO:0007744|PDB:1A2N}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FLUORINATED ANALOG OF
RP THE REACTION TETRAHEDRAL INTERMEDIATE.
RX PubMed=9485407; DOI=10.1021/bi9722608;
RA Skarzynski T., Kim D.H., Lees W.J., Walsh C.T., Duncan K.;
RT "Stereochemical course of enzymatic enolpyruvyl transfer and catalytic
RT conformation of the active site revealed by the crystal structure of the
RT fluorinated analogue of the reaction tetrahedral intermediate bound to the
RT active site of the C115A mutant of MurA.";
RL Biochemistry 37:2572-2577(1998).
RN [8] {ECO:0007744|PDB:3KQJ, ECO:0007744|PDB:3KR6}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYLGLUCOSAMINE AND FOSFOMYCIN, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND ACTIVE SITE.
RX PubMed=20392080; DOI=10.1021/bi100365b;
RA Han H., Yang Y., Olesen S.H., Becker A., Betzi S., Schoenbrunn E.;
RT "The fungal product terreic acid is a covalent inhibitor of the bacterial
RT cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-
RT carboxyvinyltransferase (MurA).";
RL Biochemistry 49:4276-4282(2010).
RN [9] {ECO:0007744|PDB:3SWD}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-418 IN COMPLEX WITH SUBSTRATE
RP ANALOG, ACTIVE SITE, AND FORMATION OF COVALENT REACTION INTERMEDIATE.
RX PubMed=22378791; DOI=10.1074/jbc.m112.342725;
RA Zhu J.Y., Yang Y., Han H., Betzi S., Olesen S.H., Marsilio F.,
RA Schoenbrunn E.;
RT "Functional consequence of covalent reaction of phosphoenolpyruvate with
RT UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).";
RL J. Biol. Chem. 287:12657-12667(2012).
CC -!- FUNCTION: Cell wall formation (PubMed:1512209). Adds enolpyruvyl to
CC UDP-N-acetylglucosamine (PubMed:1512209, PubMed:20392080). Target for
CC the antibiotic fosfomycin. {ECO:0000269|PubMed:1512209,
CC ECO:0000269|PubMed:20392080}.
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 ECO:0000269|PubMed:1512209, ECO:0000269|PubMed:20392080};
CC -!- ACTIVITY REGULATION: Competitively inhibited by UDP-N-acetylglucosamine
CC 3'-phosphate, with a Ki of 7 uM (PubMed:21445328). In vitro inhibited
CC by covalent binding of fosfomycin and the fungal product terreic acid
CC in the presence of substrate UDP-N-acetylglucosamine, with an
CC inactivation rate constant of 102 M(-1)sec(-1) for terreic acid
CC (PubMed:20392080). {ECO:0000269|PubMed:20392080,
CC ECO:0000269|PubMed:21445328}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for UDP-N-acetylglucosamine {ECO:0000269|PubMed:21445328};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000269|PubMed:1512209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR EMBL; M92358; AAA24187.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57990.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76221.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77233.1; -; Genomic_DNA.
DR EMBL; AB028039; BAA78107.1; -; Genomic_DNA.
DR PIR; A44917; A44917.
DR RefSeq; NP_417656.1; NC_000913.3.
DR RefSeq; WP_000357259.1; NZ_STEB01000012.1.
DR PDB; 1A2N; X-ray; 2.80 A; A=1-419.
DR PDB; 1UAE; X-ray; 1.80 A; A=1-419.
DR PDB; 2Z2C; X-ray; 2.05 A; A/B/C/D=1-419.
DR PDB; 3ISS; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-418.
DR PDB; 3KQJ; X-ray; 1.70 A; A=1-419.
DR PDB; 3KR6; X-ray; 1.70 A; A=1-419.
DR PDB; 3SWD; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-418.
DR PDBsum; 1A2N; -.
DR PDBsum; 1UAE; -.
DR PDBsum; 2Z2C; -.
DR PDBsum; 3ISS; -.
DR PDBsum; 3KQJ; -.
DR PDBsum; 3KR6; -.
DR PDBsum; 3SWD; -.
DR AlphaFoldDB; P0A749; -.
DR SMR; P0A749; -.
DR BioGRID; 4262438; 644.
DR BioGRID; 852016; 3.
DR DIP; DIP-48060N; -.
DR IntAct; P0A749; 25.
DR STRING; 511145.b3189; -.
DR BindingDB; P0A749; -.
DR ChEMBL; CHEMBL1984; -.
DR DrugBank; DB00828; Fosfomycin.
DR DrugCentral; P0A749; -.
DR jPOST; P0A749; -.
DR PaxDb; P0A749; -.
DR PRIDE; P0A749; -.
DR EnsemblBacteria; AAC76221; AAC76221; b3189.
DR EnsemblBacteria; BAE77233; BAE77233; BAE77233.
DR GeneID; 66672909; -.
DR GeneID; 947703; -.
DR KEGG; ecj:JW3156; -.
DR KEGG; eco:b3189; -.
DR PATRIC; fig|1411691.4.peg.3542; -.
DR EchoBASE; EB1333; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR InParanoid; P0A749; -.
DR OMA; CDPHRAT; -.
DR PhylomeDB; P0A749; -.
DR BioCyc; EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MON; -.
DR BioCyc; MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MON; -.
DR BRENDA; 2.5.1.7; 2026.
DR SABIO-RK; P0A749; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P0A749; -.
DR PRO; PR:P0A749; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW Peptidoglycan synthesis; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178870"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0000269|PubMed:8994972, ECO:0000305|PubMed:22378791,
FT ECO:0007744|PDB:1UAE, ECO:0007744|PDB:3KR6"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000305|PubMed:20392080,
FT ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3KR6,
FT ECO:0007744|PDB:3SWD"
FT BINDING 91
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0007744|PDB:3KR6"
FT BINDING 120..124
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6"
FT BINDING 160..163
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6"
FT BINDING 305
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6"
FT BINDING 327
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0007744|PDB:3KR6"
FT MOD_RES 115
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000305|PubMed:22378791"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2Z2C"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3SWD"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2Z2C"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2Z2C"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3ISS"
FT TURN 329..333
FT /evidence="ECO:0007829|PDB:2Z2C"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:3KQJ"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:3KQJ"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3ISS"
FT HELIX 402..408
FT /evidence="ECO:0007829|PDB:3KQJ"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:3KQJ"
SQ SEQUENCE 419 AA; 44818 MW; 6B75A842255E53F7 CRC64;
MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV DTSMKLLSQL
GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL VARFGQGQVS LPGGCTIGAR
PVDLHISGLE QLGATIKLEE GYVKASVDGR LKGAHIVMDK VSVGATVTIM CAATLAEGTT
IIENAAREPE IVDTANFLIT LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV
AAAISRGKII CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP
AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN TVICHGVEKL
SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE RIEDKLRALG ANIERVKGE
