Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A749

- MURA_ECOLI

UniProt

P0A749 - MURA_ECOLI

Protein

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene

murA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic fosfomycin.1 PublicationUniRule annotation

    Catalytic activityi

    Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.1 PublicationUniRule annotation

    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

    Pathwayi

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. peptidoglycan biosynthetic process Source: EcoCyc
    4. regulation of cell shape Source: UniProtKB-KW
    5. UDP-N-acetylgalactosamine biosynthetic process Source: InterPro

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11358. murA.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A749.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00790.
    OMAiHGLEQMG.
    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

    MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV    50
    DTSMKLLSQL GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL 100
    VARFGQGQVS LPGGCTIGAR PVDLHISGLE QLGATIKLEE GYVKASVDGR 150
    LKGAHIVMDK VSVGATVTIM CAATLAEGTT IIENAAREPE IVDTANFLIT 200
    LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV AAAISRGKII 250
    CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP 300
    AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN 350
    TVICHGVEKL SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE 400
    RIEDKLRALG ANIERVKGE 419
    Length:419
    Mass (Da):44,818
    Last modified:June 7, 2005 - v1
    Checksum:i6B75A842255E53F7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491374.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76221; AAC76221; b3189.
    BAE77233; BAE77233; BAE77233.
    GeneIDi12933444.
    947703.
    KEGGiecj:Y75_p3109.
    eco:b3189.
    PATRICi32121798. VBIEscCol129921_3283.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A44917.
    RefSeqi NP_417656.1. NC_000913.3.
    YP_491374.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A2N X-ray 2.80 A 1-419 [» ]
    1UAE X-ray 1.80 A 1-419 [» ]
    2Z2C X-ray 2.05 A/B/C/D 1-419 [» ]
    3ISS X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L 1-418 [» ]
    3KQJ X-ray 1.70 A 1-419 [» ]
    3KR6 X-ray 1.70 A 1-419 [» ]
    3SWD X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L 1-418 [» ]
    ProteinModelPortali P0A749.
    SMRi P0A749. Positions 1-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48060N.
    IntActi P0A749. 23 interactions.
    MINTi MINT-1224932.
    STRINGi 511145.b3189.

    Chemistry

    BindingDBi P0A749.
    ChEMBLi CHEMBL1984.
    DrugBanki DB00828. Fosfomycin.

    Proteomic databases

    PaxDbi P0A749.
    PRIDEi P0A749.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76221 ; AAC76221 ; b3189 .
    BAE77233 ; BAE77233 ; BAE77233 .
    GeneIDi 12933444.
    947703.
    KEGGi ecj:Y75_p3109.
    eco:b3189.
    PATRICi 32121798. VBIEscCol129921_3283.

    Organism-specific databases

    EchoBASEi EB1333.
    EcoGenei EG11358. murA.

    Phylogenomic databases

    eggNOGi COG0766.
    HOGENOMi HOG000075602.
    KOi K00790.
    OMAi HGLEQMG.
    OrthoDBi EOG68M4GK.
    PhylomeDBi P0A749.

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
    ECOL316407:JW3156-MONOMER.
    MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER.
    BRENDAi 2.5.1.7. 2026.

    Miscellaneous databases

    EvolutionaryTracei P0A749.
    PROi P0A749.

    Gene expression databases

    Genevestigatori P0A749.

    Family and domain databases

    Gene3Di 3.65.10.10. 2 hits.
    HAMAPi MF_00111. MurA.
    InterProi IPR001986. Enolpyruvate_Tfrase_dom.
    IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
    IPR005750. UDP_GlcNAc_COvinyl_MurA.
    [Graphical view ]
    PANTHERi PTHR21090:SF4. PTHR21090:SF4. 1 hit.
    Pfami PF00275. EPSP_synthase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55205. SSF55205. 1 hit.
    TIGRFAMsi TIGR01072. murA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 98 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