MURA_ENTCC
ID MURA_ENTCC Reviewed; 419 AA.
AC P33038; D5CCD2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 153.
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=ECL_04571;
OS Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=716541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1577165; DOI=10.1016/0014-5793(92)80255-f;
RA Wanke C., Falchetto R., Amrhein N.;
RT "The UDP-N-acetylglucosamine 1-carboxyvinyl-transferase of Enterobacter
RT cloacae. Molecular cloning, sequencing of the gene and overexpression of
RT the enzyme.";
RL FEBS Lett. 301:271-276(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC 279-56;
RX PubMed=20207761; DOI=10.1128/jb.00067-10;
RA Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT strain ATCC 13047.";
RL J. Bacteriol. 192:2463-2464(2010).
RN [3] {ECO:0007744|PDB:1NAW}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8805592; DOI=10.1016/s0969-2126(96)00113-x;
RA Schoenbrunn E., Sack S., Eschenburg S., Perrakis A., Krekel N.,
RA Mandelkow E.;
RT "Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the
RT target of the antibiotic fosfomycin.";
RL Structure 4:1065-1075(1996).
RN [4] {ECO:0007744|PDB:1DLG}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANT SER-115.
RX PubMed=10694381; DOI=10.1021/bi991091j;
RA Schoenbrunn E., Eschenburg S., Krekel F., Luger K., Amrhein N.;
RT "Role of the loop containing residue 115 in the induced-fit mechanism of
RT the bacterial cell wall biosynthetic enzyme murA.";
RL Biochemistry 39:2164-2173(2000).
RN [5] {ECO:0007744|PDB:1EJC, ECO:0007744|PDB:1EJD}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=10842342;
RX DOI=10.1002/(sici)1097-0134(20000801)40:2<290::aid-prot90>3.0.co;2-0;
RA Eschenburg S., Schoenbrunn E.;
RT "Comparative X-ray analysis of the un-liganded fosfomycin-target murA.";
RL Proteins 40:290-298(2000).
RN [6] {ECO:0007744|PDB:3KQA, ECO:0007744|PDB:3LTH}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYLGLUCOSAMINE; FOSFOMYCIN AND TERREIC ACID, FUNCTION, CATALYTIC
RP ACTIVITY, 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 [7] {ECO:0007744|PDB:3SPB, ECO:0007744|PDB:3SU9, ECO:0007744|PDB:3SWA, ECO:0007744|PDB:3SWI, ECO:0007744|PDB:3SWQ, ECO:0007744|PDB:3UPK, ECO:0007744|PDB:3V4T, ECO:0007744|PDB:3V5V}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF WILD TYPE AND MUTANTS ASP-115 AND
RP ALA-120 IN COMPLEXES WITH UDP-N-ACETYLGLUCOSAMINE AND SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, FORMATION OF COVALENT REACTION
RP INTERMEDIATE, MUTAGENESIS OF CYS-115 AND ARG-120, AND REACTION MECHANISM.
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. Adds enolpyruvyl to UDP-N-
CC acetylglucosamine (PubMed:20392080, PubMed:22378791). Target for the
CC antibiotic fosfomycin. {ECO:0000269|PubMed:20392080,
CC ECO:0000269|PubMed:22378791}.
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:20392080, ECO:0000269|PubMed:22378791};
CC -!- ACTIVITY REGULATION: In vitro inhibited by covalent binding of
CC fosfomycin and the fungal product terreic acid in the presence of
CC substrate UDP-N-acetylglucosamine, with an inactivation rate constant
CC of 130 M(-1)sec(-1) for terreic acid. {ECO:0000269|PubMed:20392080}.
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; Z11835; CAA77856.1; -; Genomic_DNA.
DR EMBL; CP001918; ADF64099.1; -; Genomic_DNA.
DR PIR; S22372; S22372.
DR RefSeq; WP_013098931.1; NC_014121.1.
DR RefSeq; YP_003615048.1; NC_014121.1.
DR PDB; 1DLG; X-ray; 1.90 A; A/B=1-419.
DR PDB; 1EJC; X-ray; 1.80 A; A=1-419.
DR PDB; 1EJD; X-ray; 1.55 A; A/B=1-419.
DR PDB; 1EYN; X-ray; 1.70 A; A=1-419.
DR PDB; 1NAW; X-ray; 2.00 A; A/B=1-419.
DR PDB; 1Q3G; X-ray; 2.65 A; A/B/C/D/E/F/G/H/I/J/K/L/W/X/Y/Z=1-419.
DR PDB; 1RYW; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-419.
DR PDB; 1YBG; X-ray; 2.60 A; A/B/C/D=1-419.
DR PDB; 3KQA; X-ray; 2.25 A; A/B/C/D=1-419.
DR PDB; 3LTH; X-ray; 1.75 A; A=1-419.
DR PDB; 3SPB; X-ray; 2.30 A; A/B/C/D=1-419.
DR PDB; 3SU9; X-ray; 2.20 A; A=1-419.
DR PDB; 3SWA; X-ray; 1.90 A; A/B=1-419.
DR PDB; 3SWI; X-ray; 2.80 A; A=1-419.
DR PDB; 3SWQ; X-ray; 1.83 A; A=1-419.
DR PDB; 3UPK; X-ray; 2.00 A; A=1-419.
DR PDB; 3V4T; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-419.
DR PDB; 3V5V; X-ray; 2.70 A; A/B/C/D=1-419.
DR PDB; 4E7B; X-ray; 2.00 A; A/B/C/D=1-419.
DR PDB; 4E7C; X-ray; 2.10 A; A/B/C/D=1-419.
DR PDB; 4E7D; X-ray; 2.50 A; A/B/C/D=1-419.
DR PDB; 4E7E; X-ray; 2.30 A; A/B/C/D=1-419.
DR PDB; 4E7F; X-ray; 2.15 A; A/B/C/D=1-419.
DR PDB; 4E7G; X-ray; 1.60 A; A=1-419.
DR PDB; 4EII; X-ray; 1.95 A; A=1-419.
DR PDBsum; 1DLG; -.
DR PDBsum; 1EJC; -.
DR PDBsum; 1EJD; -.
DR PDBsum; 1EYN; -.
DR PDBsum; 1NAW; -.
DR PDBsum; 1Q3G; -.
DR PDBsum; 1RYW; -.
DR PDBsum; 1YBG; -.
DR PDBsum; 3KQA; -.
DR PDBsum; 3LTH; -.
DR PDBsum; 3SPB; -.
DR PDBsum; 3SU9; -.
DR PDBsum; 3SWA; -.
DR PDBsum; 3SWI; -.
DR PDBsum; 3SWQ; -.
DR PDBsum; 3UPK; -.
DR PDBsum; 3V4T; -.
DR PDBsum; 3V5V; -.
DR PDBsum; 4E7B; -.
DR PDBsum; 4E7C; -.
DR PDBsum; 4E7D; -.
DR PDBsum; 4E7E; -.
DR PDBsum; 4E7F; -.
DR PDBsum; 4E7G; -.
DR PDBsum; 4EII; -.
DR AlphaFoldDB; P33038; -.
DR SMR; P33038; -.
DR STRING; 716541.ECL_04571; -.
DR BindingDB; P33038; -.
DR DrugBank; DB01879; (S)-2-{Methyl-[2-(Naphthalene-2-Sulfonylamino)-5-(Naphthalene-2-Sulfonyloxy)-Benzoyl]-Amino}-Succinicacid.
DR DrugBank; DB04174; 3'-1-carboxy-1-phosphonooxy-ethoxy-uridine-diphosphate-N-acetylglucosamine.
DR DrugBank; DB04474; 8-anilinonaphthalene-1-sulfonic acid.
DR DrugBank; DB02435; Aminomethylcyclohexane.
DR DrugBank; DB02995; Cyclohexylammonium Ion.
DR EnsemblBacteria; ADF64099; ADF64099; ECL_04571.
DR GeneID; 60932087; -.
DR KEGG; enc:ECL_04571; -.
DR PATRIC; fig|716541.4.peg.4720; -.
DR eggNOG; COG0766; Bacteria.
DR HOGENOM; CLU_027387_0_0_6; -.
DR OMA; CDPHRAT; -.
DR BRENDA; 2.5.1.7; 155.
DR SABIO-RK; P33038; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P33038; -.
DR PRO; PR:P33038; -.
DR Proteomes; UP000002363; 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 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; Transferase.
FT CHAIN 1..419
FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT /id="PRO_0000178873"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:20392080,
FT ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH"
FT BINDING 22..23
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000305|PubMed:22378791,
FT ECO:0007744|PDB:3SWQ"
FT BINDING 91
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
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:3LTH,
FT ECO:0007744|PDB:3SWQ"
FT BINDING 160..163
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22378791,
FT ECO:0007744|PDB:3SWQ"
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:3LTH,
FT ECO:0007744|PDB:3SWQ"
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:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH,
FT ECO:0007744|PDB:3SWQ"
FT MOD_RES 115
FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT /evidence="ECO:0000269|PubMed:22378791"
FT MUTAGEN 115
FT /note="C->D: Significantly lower binding of
FT phosphoenolpyruvate."
FT /evidence="ECO:0000269|PubMed:22378791"
FT MUTAGEN 115
FT /note="C->S: Loss of activity, but not of substrate
FT binding."
FT MUTAGEN 120
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22378791"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3SWA"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4E7B"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:1EJD"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4E7G"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4E7G"
FT TURN 329..333
FT /evidence="ECO:0007829|PDB:3V4T"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4E7G"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 393..398
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1EJD"
FT HELIX 402..407
FT /evidence="ECO:0007829|PDB:1EJD"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:1EJD"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:1EJD"
SQ SEQUENCE 419 AA; 44777 MW; 19C976B098245A68 CRC64;
MDKFRVQGPT RLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDI DTTMKLLTQL
GTKVERNGSV WIDASNVNNF SAPYDLVKTM RASIWALGPL VARFGQGQVS LPGGCAIGAR
PVDLHIFGLE KLGAEIKLEE GYVKASVNGR LKGAHIVMDK VSVGATVTIM SAATLAEGTT
IIENAAREPE IVDTANFLVA LGAKISGQGT DRITIEGVER LGGGVYRVLP DRIETGTFLV
AAAISGGKIV CRNAQPDTLD AVLAKLREAG ADIETGEDWI SLDMHGKRPK AVTVRTAPHP
AFPTDMQAQF TLLNLVAEGT GVITETIFEN RFMHVPELIR MGAHAEIESN TVICHGVEKL
SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE RIEDKLRALG ANIERVKGE
