ID   MURQ_THEPX              Reviewed;         302 AA.
AC   B0K1N2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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};
GN   OrderedLocusNames=Teth514_0172;
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter;
OC   unclassified Thermoanaerobacter.
OX   NCBI_TaxID=399726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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. {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; N-acetylmuramate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00068}.
CC   -!- SUBUNIT: Homodimer. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000923; ABY91491.1; -; Genomic_DNA.
DR   RefSeq; WP_009051939.1; NC_010320.1.
DR   AlphaFoldDB; B0K1N2; -.
DR   SMR; B0K1N2; -.
DR   EnsemblBacteria; ABY91491; ABY91491; Teth514_0172.
DR   KEGG; tex:Teth514_0172; -.
DR   HOGENOM; CLU_049049_1_1_9; -.
DR   OMA; CPPTFCT; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000002155; 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: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   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; PF13580; SIS_2; 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..302
FT                   /note="N-acetylmuramic acid 6-phosphate etherase"
FT                   /id="PRO_1000092321"
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   302 AA;  32785 MW;  6AAC3392B616CC8D CRC64;
     MDLDKLITEG RNPDTLDIDR LSTEDMLKKI NNEDKKVPIA VEKEIPNIAK AVDIIAEKLK
     QGGRLIYIGA GTSGRLGILD ASECPPTFGV DPEMVQGIIA GGDVAIRRSV EDAEDKEDLG
     KEDLKKKNLS SKDVVVGIAA SGRTPYVLGA LRYAKEVGAH TVGISCNPDS EMKKIVDIMI
     APVVGPEVIM GSTRMKAGTA QKLVLNMLST GAMIKLGKVY SNLMVDVKAT NEKLINRAKR
     IVKLATDADE KVIEKILKET NYNVKLTILM ILTGLNQNKA KELLDRSNGY IAKALMLNEN
     KS