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Protein

N-acetylmuramic acid 6-phosphate etherase

Gene

murQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei83 – 831Proton donor1 Publication
    Active sitei114 – 11411 Publication

    GO - Molecular functioni

    • carbohydrate 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-HAMAP
    • N-acetylmuramic acid catabolic process Source: UniProtKB-UniPathway
    • peptidoglycan turnover Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:G7263-MONOMER.
    ECOL316407:JW2421-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14162. murQ.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831E → A: 10000-fold reduction in catalytic activity. 1 Publication
    Mutagenesisi83 – 831E → Q: Loss of catalytic activity. 1 Publication
    Mutagenesisi114 – 1141E → Q: 2000-fold reduction in catalytic activity and 4-fold increase in substrate affinity. 1 Publication
    Mutagenesisi115 – 1151D → N: 7-fold reduction in catalytic activity and 1.5-fold increase in substrate affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298N-acetylmuramic acid 6-phosphate etherasePRO_0000214829Add
    BLAST

    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 interactions.
    IntActiP76535. 6 interactions.
    STRINGi511145.b2428.

    Structurei

    3D structure databases

    ProteinModelPortaliP76535.
    SMRiP76535. Positions 6-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 218164SISAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SIS domain.Curated

    Phylogenomic databases

    eggNOGiENOG4105E15. Bacteria.
    COG2103. LUCA.
    HOGENOMiHOG000084045.
    InParanoidiP76535.
    KOiK07106.
    OMAiQHQGFIR.
    OrthoDBiEOG6DG2VH.
    PhylomeDBiP76535.

    Family and domain databases

    HAMAPiMF_00068. MurQ.
    InterProiIPR005488. Etherase_MurQ.
    IPR005486. Glucokinase_regulatory_CS.
    IPR001347. SIS.
    [Graphical view]
    PfamiPF01380. SIS. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00274. TIGR00274. 1 hit.
    PROSITEiPS01272. GCKR. 1 hit.
    PS51464. SIS. 1 hit.
    [Graphical view]

    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.
    PATRICi32120241. VBIEscCol129921_2523.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliP76535.
    SMRiP76535. Positions 6-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260569. 7 interactions.
    IntActiP76535. 6 interactions.
    STRINGi511145.b2428.

    Proteomic databases

    EPDiP76535.
    PaxDbiP76535.
    PRIDEiP76535.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75481; AAC75481; b2428.
    BAA16312; BAA16312; BAA16312.
    GeneIDi946893.
    KEGGiecj:JW2421.
    eco:b2428.
    PATRICi32120241. VBIEscCol129921_2523.

    Organism-specific databases

    EchoBASEiEB3914.
    EcoGeneiEG14162. murQ.

    Phylogenomic databases

    eggNOGiENOG4105E15. Bacteria.
    COG2103. LUCA.
    HOGENOMiHOG000084045.
    InParanoidiP76535.
    KOiK07106.
    OMAiQHQGFIR.
    OrthoDBiEOG6DG2VH.
    PhylomeDBiP76535.

    Enzyme and pathway databases

    UniPathwayiUPA00342.
    UPA00343.
    UPA00544.
    BioCyciEcoCyc:G7263-MONOMER.
    ECOL316407:JW2421-MONOMER.
    MetaCyc:G7263-MONOMER.

    Miscellaneous databases

    PROiP76535.

    Family and domain databases

    HAMAPiMF_00068. MurQ.
    InterProiIPR005488. Etherase_MurQ.
    IPR005486. Glucokinase_regulatory_CS.
    IPR001347. SIS.
    [Graphical view]
    PfamiPF01380. SIS. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00274. TIGR00274. 1 hit.
    PROSITEiPS01272. GCKR. 1 hit.
    PS51464. SIS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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], SEQUENCE REVISION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
      Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
      Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: B / BL21.
    5. "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli 'etherase'."
      Jaeger T., Arsic M., Mayer C.
      J. Biol. Chem. 280:30100-30106(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
    6. "MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall."
      Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T.
      J. Bacteriol. 188:1660-1662(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL WALL RECYCLING.
    7. "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling."
      Hadi T., Dahl U., Mayer C., Tanner M.E.
      Biochemistry 47:11547-11558(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC PARAMETERS, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, MUTAGENESIS OF GLU-83; GLU-114 AND ASP-115.
    8. "The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli."
      Jaeger T., Mayer C.
      J. Bacteriol. 190:6598-6608(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiMURQ_ECOLI
    AccessioniPrimary (citable) accession number: P76535
    Secondary accession number(s): P76965, P76966, P76967
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: March 16, 2016
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    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

    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.