Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetylmuramic acid 6-phosphate etherase

Gene

murQ

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

Functioni

Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Is required for growth on MurNAc as the sole source of carbon and energy. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.2 Publications

Miscellaneous

A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product.

Catalytic activityi

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O.1 Publication

Kineticsi

kcat is 5.7 s(-1).
  1. KM=1.20 mM for N-acetylmuramic acid 6-phosphate1 Publication

    Pathwayi: 1,6-anhydro-N-acetylmuramate degradation

    This protein is involved in the pathway 1,6-anhydro-N-acetylmuramate degradation, which is part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the pathway 1,6-anhydro-N-acetylmuramate degradation and in Amino-sugar metabolism.

    Pathwayi: N-acetylmuramate degradation

    This protein is involved in the pathway N-acetylmuramate degradation, which is part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the pathway N-acetylmuramate degradation and in Amino-sugar metabolism.

    Pathwayi: peptidoglycan recycling

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei83Proton donor1 Publication1
    Active sitei1141 Publication1

    GO - Molecular functioni

    • carbohydrate derivative binding Source: InterPro
    • carbon-oxygen lyase activity Source: EcoCyc
    • ether hydrolase activity Source: EcoliWiki

    GO - Biological processi

    • 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process Source: UniProtKB-UniPathway
    • amino sugar catabolic process Source: EcoCyc
    • carbohydrate metabolic process Source: UniProtKB-KW
    • N-acetylmuramic acid catabolic process Source: UniProtKB-UniPathway
    • peptidoglycan turnover Source: EcoCyc

    Keywordsi

    Molecular functionLyase
    Biological processCarbohydrate metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:G7263-MONOMER
    MetaCyc:G7263-MONOMER
    UniPathwayiUPA00342
    UPA00343
    UPA00544

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmuramic acid 6-phosphate etherase (EC:4.2.1.126)
    Short name:
    MurNAc-6-P etherase
    Alternative name(s):
    N-acetylmuramic acid 6-phosphate hydrolase
    N-acetylmuramic acid 6-phosphate lyase
    Gene namesi
    Name:murQ
    Synonyms:yfeU
    Ordered Locus Names:b2428, JW2421
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14162 murQ

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi83E → A: 10000-fold reduction in catalytic activity. 1 Publication1
    Mutagenesisi83E → Q: Loss of catalytic activity. 1 Publication1
    Mutagenesisi114E → Q: 2000-fold reduction in catalytic activity and 4-fold increase in substrate affinity. 1 Publication1
    Mutagenesisi115D → N: 7-fold reduction in catalytic activity and 1.5-fold increase in substrate affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002148291 – 298N-acetylmuramic acid 6-phosphate etheraseAdd BLAST298

    Proteomic databases

    EPDiP76535
    PaxDbiP76535
    PRIDEiP76535

    Expressioni

    Inductioni

    Induced by MurNAc 6-phosphate that releases the repressor MurR from the DNA. Also up-regulated by the cAMP receptor protein crp via the binding of crp-cAMP to a class I site upstream of the murQ promoter. Repressed by MurR in the absence of MurNAc 6-phosphate.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4260569, 7 interactors
    IntActiP76535, 6 interactors
    STRINGi316385.ECDH10B_2593

    Structurei

    3D structure databases

    ProteinModelPortaliP76535
    SMRiP76535
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini55 – 218SISAdd BLAST164

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105E15 Bacteria
    COG2103 LUCA
    HOGENOMiHOG000084045
    InParanoidiP76535
    KOiK07106
    OMAiECPPTFC
    PhylomeDBiP76535

    Family and domain databases

    CDDicd05007 SIS_Etherase, 1 hit
    HAMAPiMF_00068 MurQ, 1 hit
    InterProiView protein in InterPro
    IPR005488 Etherase_MurQ
    IPR005486 Glucokinase_regulatory_CS
    IPR001347 SIS
    PANTHERiPTHR10088:SF5 PTHR10088:SF5, 1 hit
    PfamiView protein in Pfam
    PF01380 SIS, 1 hit
    TIGRFAMsiTIGR00274 TIGR00274, 1 hit
    PROSITEiView protein in PROSITE
    PS01272 GCKR, 1 hit
    PS51464 SIS, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P76535-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQFEKMITEG SNTASAEIDR VSTLEMCRII NDEDKTVPLA VERVLPDIAA
    60 70 80 90 100
    AIDVIHAQVS GGGRLIYLGA GTSGRLGILD ASECPPTYGV KPGLVVGLIA
    110 120 130 140 150
    GGEYAIQHAV EGAEDSREGG VNDLKNINLT AQDVVVGIAA SGRTPYVIAG
    160 170 180 190 200
    LEYARQLGCR TVGISCNPGS AVSTTAEFAI TPIVGAEVVT GSSRMKAGTA
    210 220 230 240 250
    QKLVLNMLST GLMIKSGKVF GNLMVDVVAT NEKLHVRQVN IVKNATGCSA
    260 270 280 290
    EQAEAALIAC ERNCKTAIVM VLKNLDAAEA KKRLDQHGGF IRQVLDKE
    Length:298
    Mass (Da):31,220
    Last modified:February 1, 1997 - v1
    Checksum:i34FE8F878E8B3077
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC75481.1
    AP009048 Genomic DNA Translation: BAA16312.2
    PIRiC65017
    RefSeqiNP_416923.1, NC_000913.3
    WP_001159160.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75481; AAC75481; b2428
    BAA16312; BAA16312; BAA16312
    GeneIDi946893
    KEGGiecj:JW2421
    eco:b2428
    PATRICifig|1411691.4.peg.4303

    Similar proteinsi

    Entry informationi

    Entry nameiMURQ_ECOLI
    AccessioniPrimary (citable) accession number: P76535
    Secondary accession number(s): P76965, P76966, P76967
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: March 28, 2018
    This is version 134 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health