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Protein

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene

murA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic fosfomycin.UniRule annotation1 Publication

Catalytic activityi

Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.UniRule annotation1 Publication

Enzyme regulationi

Competitively inhibited by UDP-N-acetylglucosamine 3'-phosphate, with a Ki of 7 µM.1 Publication

Kineticsi

  1. KM=15 µM for UDP-N-acetylglucosamine1 Publication

    Pathway: peptidoglycan biosynthesis

    This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei115 – 1151Proton donor

    GO - Molecular functioni

    • UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    Pyruvate

    Enzyme and pathway databases

    BioCyciEcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
    ECOL316407:JW3156-MONOMER.
    MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
    BRENDAi2.5.1.7. 2026.
    UniPathwayiUPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylglucosamine 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.7UniRule annotation)
    Alternative name(s):
    Enoylpyruvate transferaseUniRule annotation
    UDP-N-acetylglucosamine enolpyruvyl transferaseUniRule annotation
    Short name:
    EPTUniRule annotation
    Gene namesi
    Name:murAUniRule annotation
    Synonyms:murZ
    Ordered Locus Names:b3189, JW3156
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11358. murA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry

    DrugBankiDB00828. Fosfomycin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419UDP-N-acetylglucosamine 1-carboxyvinyltransferasePRO_0000178870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 11512-(S-cysteinyl)pyruvic acid O-phosphothioketal

    Proteomic databases

    PaxDbiP0A749.
    PRIDEiP0A749.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48060N.
    IntActiP0A749. 23 interactions.
    MINTiMINT-1224932.
    STRINGi511145.b3189.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Beta strandi14 – 174Combined sources
    Helixi22 – 3110Combined sources
    Helixi32 – 343Combined sources
    Beta strandi35 – 373Combined sources
    Beta strandi39 – 435Combined sources
    Helixi48 – 5912Combined sources
    Beta strandi63 – 653Combined sources
    Beta strandi70 – 734Combined sources
    Helixi74 – 763Combined sources
    Helixi84 – 874Combined sources
    Helixi92 – 965Combined sources
    Helixi97 – 1048Combined sources
    Beta strandi105 – 1106Combined sources
    Beta strandi116 – 1183Combined sources
    Helixi123 – 1319Combined sources
    Beta strandi135 – 1395Combined sources
    Beta strandi142 – 1465Combined sources
    Beta strandi148 – 1503Combined sources
    Beta strandi155 – 1573Combined sources
    Helixi163 – 17311Combined sources
    Beta strandi176 – 1849Combined sources
    Helixi189 – 20012Combined sources
    Beta strandi204 – 2063Combined sources
    Beta strandi210 – 2167Combined sources
    Beta strandi224 – 2274Combined sources
    Helixi232 – 24514Combined sources
    Beta strandi248 – 2536Combined sources
    Helixi256 – 2583Combined sources
    Helixi260 – 2689Combined sources
    Beta strandi272 – 2754Combined sources
    Beta strandi277 – 2837Combined sources
    Beta strandi293 – 2953Combined sources
    Helixi304 – 3063Combined sources
    Helixi307 – 31610Combined sources
    Beta strandi317 – 3248Combined sources
    Beta strandi326 – 3283Combined sources
    Turni329 – 3335Combined sources
    Helixi334 – 3396Combined sources
    Turni340 – 3423Combined sources
    Beta strandi344 – 3485Combined sources
    Beta strandi351 – 3555Combined sources
    Beta strandi364 – 3663Combined sources
    Helixi370 – 38213Combined sources
    Beta strandi383 – 3908Combined sources
    Helixi392 – 3976Combined sources
    Beta strandi399 – 4013Combined sources
    Helixi402 – 4087Combined sources
    Beta strandi412 – 4176Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A2NX-ray2.80A1-419[»]
    1UAEX-ray1.80A1-419[»]
    2Z2CX-ray2.05A/B/C/D1-419[»]
    3ISSX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
    3KQJX-ray1.70A1-419[»]
    3KR6X-ray1.70A1-419[»]
    3SWDX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
    ProteinModelPortaliP0A749.
    SMRiP0A749. Positions 1-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A749.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the EPSP synthase family. MurA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0766.
    HOGENOMiHOG000075602.
    InParanoidiP0A749.
    KOiK00790.
    OMAiIRTAPHP.
    OrthoDBiEOG68M4GK.
    PhylomeDBiP0A749.

    Family and domain databases

    Gene3Di3.65.10.10. 2 hits.
    HAMAPiMF_00111. MurA.
    InterProiIPR001986. Enolpyruvate_Tfrase_dom.
    IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
    IPR005750. UDP_GlcNAc_COvinyl_MurA.
    [Graphical view]
    PANTHERiPTHR21090:SF4. PTHR21090:SF4. 1 hit.
    PfamiPF00275. EPSP_synthase. 1 hit.
    [Graphical view]
    SUPFAMiSSF55205. SSF55205. 1 hit.
    TIGRFAMsiTIGR01072. murA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A749-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV
    60 70 80 90 100
    DTSMKLLSQL GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL
    110 120 130 140 150
    VARFGQGQVS LPGGCTIGAR PVDLHISGLE QLGATIKLEE GYVKASVDGR
    160 170 180 190 200
    LKGAHIVMDK VSVGATVTIM CAATLAEGTT IIENAAREPE IVDTANFLIT
    210 220 230 240 250
    LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV AAAISRGKII
    260 270 280 290 300
    CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP
    310 320 330 340 350
    AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN
    360 370 380 390 400
    TVICHGVEKL SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE
    410
    RIEDKLRALG ANIERVKGE
    Length:419
    Mass (Da):44,818
    Last modified:June 7, 2005 - v1
    Checksum:i6B75A842255E53F7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M92358 Genomic DNA. Translation: AAA24187.1.
    U18997 Genomic DNA. Translation: AAA57990.1.
    U00096 Genomic DNA. Translation: AAC76221.1.
    AP009048 Genomic DNA. Translation: BAE77233.1.
    AB028039 Genomic DNA. Translation: BAA78107.1.
    PIRiA44917.
    RefSeqiNP_417656.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC76221; AAC76221; b3189.
    BAE77233; BAE77233; BAE77233.
    GeneIDi947703.
    KEGGiecj:Y75_p3109.
    eco:b3189.
    PATRICi32121798. VBIEscCol129921_3283.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M92358 Genomic DNA. Translation: AAA24187.1.
    U18997 Genomic DNA. Translation: AAA57990.1.
    U00096 Genomic DNA. Translation: AAC76221.1.
    AP009048 Genomic DNA. Translation: BAE77233.1.
    AB028039 Genomic DNA. Translation: BAA78107.1.
    PIRiA44917.
    RefSeqiNP_417656.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A2NX-ray2.80A1-419[»]
    1UAEX-ray1.80A1-419[»]
    2Z2CX-ray2.05A/B/C/D1-419[»]
    3ISSX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
    3KQJX-ray1.70A1-419[»]
    3KR6X-ray1.70A1-419[»]
    3SWDX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-418[»]
    ProteinModelPortaliP0A749.
    SMRiP0A749. Positions 1-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48060N.
    IntActiP0A749. 23 interactions.
    MINTiMINT-1224932.
    STRINGi511145.b3189.

    Chemistry

    BindingDBiP0A749.
    ChEMBLiCHEMBL1984.
    DrugBankiDB00828. Fosfomycin.

    Proteomic databases

    PaxDbiP0A749.
    PRIDEiP0A749.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76221; AAC76221; b3189.
    BAE77233; BAE77233; BAE77233.
    GeneIDi947703.
    KEGGiecj:Y75_p3109.
    eco:b3189.
    PATRICi32121798. VBIEscCol129921_3283.

    Organism-specific databases

    EchoBASEiEB1333.
    EcoGeneiEG11358. murA.

    Phylogenomic databases

    eggNOGiCOG0766.
    HOGENOMiHOG000075602.
    InParanoidiP0A749.
    KOiK00790.
    OMAiIRTAPHP.
    OrthoDBiEOG68M4GK.
    PhylomeDBiP0A749.

    Enzyme and pathway databases

    UniPathwayiUPA00219.
    BioCyciEcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
    ECOL316407:JW3156-MONOMER.
    MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
    BRENDAi2.5.1.7. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A749.
    PROiP0A749.

    Family and domain databases

    Gene3Di3.65.10.10. 2 hits.
    HAMAPiMF_00111. MurA.
    InterProiIPR001986. Enolpyruvate_Tfrase_dom.
    IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
    IPR005750. UDP_GlcNAc_COvinyl_MurA.
    [Graphical view]
    PANTHERiPTHR21090:SF4. PTHR21090:SF4. 1 hit.
    PfamiPF00275. EPSP_synthase. 1 hit.
    [Graphical view]
    SUPFAMiSSF55205. SSF55205. 1 hit.
    TIGRFAMsiTIGR01072. murA. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase."
      Marquardt J.L., Siegele D.A., Kolter R., Walsh C.T.
      J. Bacteriol. 174:5748-5752(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
      Strain: K12 / AB1157.
    2. "Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26."
      Horii T., Kimura T., Sato K., Shibayama K., Ohta M.
      Antimicrob. Agents Chemother. 43:789-793(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: O26 / NGY47.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis."
      Mutschler H., Gebhardt M., Shoeman R.L., Meinhart A.
      PLoS Biol. 9:E1001033-E1001033(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin."
      Skarzynski T., Mistry A., Wonacott A., Hutchinson S.E., Kelly V.A., Duncan K.
      Structure 4:1465-1474(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FOSFOMYCIN.
    7. "Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA."
      Skarzynski T., Kim D.H., Lees W.J., Walsh C.T., Duncan K.
      Biochemistry 37:2572-2577(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiMURA_ECOLI
    AccessioniPrimary (citable) accession number: P0A749
    Secondary accession number(s): P28909, Q2M923
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: June 24, 2015
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.