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MURQ_ECO27
ID   MURQ_ECO27              Reviewed;         298 AA.
AC   B7UGC8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000255|HAMAP-Rule:MF_00068};
DE            Short=MurNAc-6-P etherase {ECO:0000255|HAMAP-Rule:MF_00068};
DE            EC=4.2.1.126 {ECO:0000255|HAMAP-Rule:MF_00068};
DE   AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00068};
DE   AltName: Full=N-acetylmuramic acid 6-phosphate lyase {ECO:0000255|HAMAP-Rule:MF_00068};
GN   Name=murQ {ECO:0000255|HAMAP-Rule:MF_00068}; OrderedLocusNames=E2348C_2613;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether
CC       substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-
CC       lactate. Together with AnmK, is also required for the utilization of
CC       anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the
CC       medium or derived from its own cell wall murein, and thus plays a role
CC       in cell wall recycling. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-
CC         acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:26410,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16004, ChEBI:CHEBI:57513,
CC         ChEBI:CHEBI:58722; EC=4.2.1.126; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00068};
CC   -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC       degradation. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- INDUCTION: Induced by MurNAc 6-phosphate that releases the repressor
CC       MurR from the DNA. Repressed by MurR in the absence of MurNAc 6-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is
CC       suggested for the cleavage of the lactyl ether bond of MurNAc 6-
CC       phosphate, with the formation of an alpha,beta-unsaturated aldehyde
CC       intermediate with (E)-stereochemistry, followed by the syn addition of
CC       water to give product. {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00068}.
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DR   EMBL; FM180568; CAS10161.1; -; Genomic_DNA.
DR   RefSeq; WP_001175631.1; NC_011601.1.
DR   AlphaFoldDB; B7UGC8; -.
DR   SMR; B7UGC8; -.
DR   EnsemblBacteria; CAS10161; CAS10161; E2348C_2613.
DR   KEGG; ecg:E2348C_2613; -.
DR   HOGENOM; CLU_049049_1_1_6; -.
DR   OMA; CPPTFCT; -.
DR   UniPathway; UPA00342; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046348; P:amino sugar catabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR   CDD; cd05007; SIS_Etherase; 1.
DR   HAMAP; MF_00068; MurQ; 1.
DR   InterPro; IPR005488; Etherase_MurQ.
DR   InterPro; IPR005486; Glucokinase_regulatory_CS.
DR   InterPro; IPR040190; MURQ/GCKR.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10088; PTHR10088; 1.
DR   PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   TIGRFAMs; TIGR00274; TIGR00274; 1.
DR   PROSITE; PS01272; GCKR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Lyase.
FT   CHAIN           1..298
FT                   /note="N-acetylmuramic acid 6-phosphate etherase"
FT                   /id="PRO_1000118010"
FT   DOMAIN          55..218
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   298 AA;  31101 MW;  3A21CD465CEB1E81 CRC64;
     MQLEKMITEG SNAASAEIDR VSTLEMCRII NDEDKTVPLA VERVLPDIAA AIDVIHTQVS
     GGGRLIYLGA GTSGRLGILD ASECPPTYGV KPGLVVGLIA GGEYAIQHAV EGAEDSREGG
     VNDLKNIGLT AQDVVVGIAA SGRTPYVIAG LEYARQLGCR TVGISCNPGS AVSTTAEFAI
     TPVVGAEVVT GSSRMKAGTA QKLVLNMLST GLMIKSGKVF GNLMVDVVAT NEKLHVRQVN
     IVKNATGCSA EQAEAALVAC ERNCKTAIVM VLKNLDAAEA KKRLDQHGGF IRQVLDKE
 
 
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