MURQ_ECO57
ID MURQ_ECO57 Reviewed; 298 AA.
AC Q8XBJ2;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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}; Synonyms=yfeU;
GN OrderedLocusNames=Z3693, ECs3299;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57546.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36722.1; -; Genomic_DNA.
DR PIR; C91041; C91041.
DR PIR; F85885; F85885.
DR RefSeq; NP_311326.1; NC_002695.1.
DR RefSeq; WP_001175615.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XBJ2; -.
DR SMR; Q8XBJ2; -.
DR STRING; 155864.EDL933_3591; -.
DR EnsemblBacteria; AAG57546; AAG57546; Z3693.
DR EnsemblBacteria; BAB36722; BAB36722; ECs_3299.
DR GeneID; 915479; -.
DR KEGG; ece:Z3693; -.
DR KEGG; ecs:ECs_3299; -.
DR PATRIC; fig|386585.9.peg.3446; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_6; -.
DR OMA; CPPTFCT; -.
DR UniPathway; UPA00342; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT CHAIN 1..298
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_0000214830"
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; 31112 MW; 231B33A48F7E1E81 CRC64;
MQLEKMITEG SNAASAEIDR VSTLEMCRII NDEDKTVPLA VERVLPDIAA AIDVIHAQVS
GGGRLIYLGA GTSGRLGILD ASECPPTYGV KPGLVVGLIA GGEYAIQHAV EGAEDSREGG
VNDLKNIGLT AQDVVVGIAA SGRTPYVIAG LEYARQLGCR TVGISCNPGS AVSTTAEFAI
TPVVGAEVVT GSSRMKAGTA QKLVLNMLST GLMIKSGKVF GNLMVDVVAT NEKLHVRQVN
IVKNATGCNA EQAEAALIAC ERNCKTAIVM VLKNLDAAEA KKRLDQHGGF IRQVLDKE
