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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 (PubMed:1512209). Adds enolpyruvyl to UDP-N-acetylglucosamine (PubMed:1512209, PubMed:20392080). Target for the antibiotic fosfomycin.2 Publications

Catalytic activityi

Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.UniRule annotation2 Publications

Enzyme regulationi

Competitively inhibited by UDP-N-acetylglucosamine 3'-phosphate, with a Ki of 7 µM (PubMed:21445328). In vitro inhibited by covalent binding of fosfomycin and the fungal product terreic acid in the presence of substrate UDP-N-acetylglucosamine, with an inactivation rate constant of 102 M(-1)s(-1) for terreic acid (PubMed:20392080).2 Publications

Kineticsi

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

    Pathwayi: 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)DescriptionActionsGraphical viewLength
    Binding sitei91UDP-N-acetylglucosamineCombined sources1 Publication1
    Active sitei115Proton donorCombined sources1 Publication2 Publications1
    Binding sitei305UDP-N-acetylglucosamineCombined sources2 Publications1
    Binding sitei327UDP-N-acetylglucosamine; via carbonyl oxygenCombined sources1 Publication1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11358. murA.

    Subcellular locationi

    • Cytoplasm UniRule annotationCurated

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL1984.
    DrugBankiDB00828. Fosfomycin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001788701 – 419UDP-N-acetylglucosamine 1-carboxyvinyltransferaseAdd BLAST419

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1152-(S-cysteinyl)pyruvic acid O-phosphothioketal1 Publication1

    Proteomic databases

    EPDiP0A749.
    PaxDbiP0A749.
    PRIDEiP0A749.

    Interactioni

    Protein-protein interaction databases

    BioGridi4262438. 633 interactors.
    DIPiDIP-48060N.
    IntActiP0A749. 23 interactors.
    MINTiMINT-1224932.
    STRINGi511145.b3189.

    Chemistry databases

    BindingDBiP0A749.

    Structurei

    Secondary structure

    1419
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Beta strandi14 – 17Combined sources4
    Helixi22 – 31Combined sources10
    Helixi32 – 34Combined sources3
    Beta strandi35 – 37Combined sources3
    Beta strandi39 – 43Combined sources5
    Helixi48 – 59Combined sources12
    Beta strandi63 – 65Combined sources3
    Beta strandi70 – 73Combined sources4
    Helixi74 – 76Combined sources3
    Helixi84 – 87Combined sources4
    Helixi92 – 96Combined sources5
    Helixi97 – 104Combined sources8
    Beta strandi105 – 110Combined sources6
    Beta strandi116 – 118Combined sources3
    Helixi123 – 131Combined sources9
    Beta strandi135 – 139Combined sources5
    Beta strandi142 – 146Combined sources5
    Beta strandi148 – 150Combined sources3
    Beta strandi155 – 157Combined sources3
    Helixi163 – 173Combined sources11
    Beta strandi176 – 184Combined sources9
    Helixi189 – 200Combined sources12
    Beta strandi204 – 206Combined sources3
    Beta strandi210 – 216Combined sources7
    Beta strandi224 – 227Combined sources4
    Helixi232 – 245Combined sources14
    Beta strandi248 – 253Combined sources6
    Helixi256 – 258Combined sources3
    Helixi260 – 268Combined sources9
    Beta strandi272 – 275Combined sources4
    Beta strandi277 – 283Combined sources7
    Beta strandi293 – 295Combined sources3
    Helixi304 – 306Combined sources3
    Helixi307 – 316Combined sources10
    Beta strandi317 – 324Combined sources8
    Beta strandi326 – 328Combined sources3
    Turni329 – 333Combined sources5
    Helixi334 – 339Combined sources6
    Turni340 – 342Combined sources3
    Beta strandi344 – 348Combined sources5
    Beta strandi351 – 355Combined sources5
    Beta strandi364 – 366Combined sources3
    Helixi370 – 382Combined sources13
    Beta strandi383 – 390Combined sources8
    Helixi392 – 397Combined sources6
    Beta strandi399 – 401Combined sources3
    Helixi402 – 408Combined sources7
    Beta strandi412 – 417Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A749.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni22 – 23Phosphoenolpyruvate bindingCombined sources2 Publications2
    Regioni120 – 124UDP-N-acetylglucosamine bindingCombined sources2 Publications5
    Regioni160 – 163UDP-N-acetylglucosamine bindingCombined sources2 Publications4

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105CDF. Bacteria.
    COG0766. LUCA.
    HOGENOMiHOG000075602.
    InParanoidiP0A749.
    KOiK00790.
    OMAiIRTAPHP.
    PhylomeDBiP0A749.

    Family and domain databases

    CDDicd01555. UdpNAET. 1 hit.
    Gene3Di3.65.10.10. 2 hits.
    HAMAPiMF_00111. MurA. 1 hit.
    InterProiIPR001986. Enolpyruvate_Tfrase_dom.
    IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
    IPR005750. UDP_GlcNAc_COvinyl_MurA.
    [Graphical view]
    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.
    WP_000357259.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76221; AAC76221; b3189.
    BAE77233; BAE77233; BAE77233.
    GeneIDi947703.
    KEGGiecj:JW3156.
    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.
    WP_000357259.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262438. 633 interactors.
    DIPiDIP-48060N.
    IntActiP0A749. 23 interactors.
    MINTiMINT-1224932.
    STRINGi511145.b3189.

    Chemistry databases

    BindingDBiP0A749.
    ChEMBLiCHEMBL1984.
    DrugBankiDB00828. Fosfomycin.

    Proteomic databases

    EPDiP0A749.
    PaxDbiP0A749.
    PRIDEiP0A749.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76221; AAC76221; b3189.
    BAE77233; BAE77233; BAE77233.
    GeneIDi947703.
    KEGGiecj:JW3156.
    eco:b3189.
    PATRICi32121798. VBIEscCol129921_3283.

    Organism-specific databases

    EchoBASEiEB1333.
    EcoGeneiEG11358. murA.

    Phylogenomic databases

    eggNOGiENOG4105CDF. Bacteria.
    COG0766. LUCA.
    HOGENOMiHOG000075602.
    InParanoidiP0A749.
    KOiK00790.
    OMAiIRTAPHP.
    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

    CDDicd01555. UdpNAET. 1 hit.
    Gene3Di3.65.10.10. 2 hits.
    HAMAPiMF_00111. MurA. 1 hit.
    InterProiIPR001986. Enolpyruvate_Tfrase_dom.
    IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
    IPR005750. UDP_GlcNAc_COvinyl_MurA.
    [Graphical view]
    PfamiPF00275. EPSP_synthase. 1 hit.
    [Graphical view]
    SUPFAMiSSF55205. SSF55205. 1 hit.
    TIGRFAMsiTIGR01072. murA. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 114 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

    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 one 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.