ID   MURQ_RHOBA              Reviewed;         302 AA.
AC   Q7UNL6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=RB7514;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
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DR   EMBL; BX294146; CAD75403.1; -; Genomic_DNA.
DR   RefSeq; NP_867856.1; NC_005027.1.
DR   RefSeq; WP_011121425.1; NC_005027.1.
DR   AlphaFoldDB; Q7UNL6; -.
DR   SMR; Q7UNL6; -.
DR   STRING; 243090.RB7514; -.
DR   EnsemblBacteria; CAD75403; CAD75403; RB7514.
DR   KEGG; rba:RB7514; -.
DR   PATRIC; fig|243090.15.peg.3628; -.
DR   eggNOG; COG2103; Bacteria.
DR   HOGENOM; CLU_049049_1_1_0; -.
DR   InParanoid; Q7UNL6; -.
DR   OMA; CPPTFCT; -.
DR   OrthoDB; 1100044at2; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IBA:GO_Central.
DR   GO; GO:0016803; F:ether hydrolase activity; IBA:GO_Central.
DR   GO; GO:0046348; P:amino sugar catabolic process; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..302
FT                   /note="N-acetylmuramic acid 6-phosphate etherase"
FT                   /id="PRO_0000249646"
FT   DOMAIN          57..220
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   302 AA;  32061 MW;  C913AA2CE63525C6 CRC64;
     MLNQLNQLTT EASNPASAQI DSLSALQIVQ LINQQDALVA AAVNTQAEMI AEAVDVIADR
     FRSNGRLIYL GAGTSGRLGV LDASECPPTF RTPPEMVVGV IAGGPEALTR AIEGAEDHPE
     FAERDLAKIN LSSNDVLVGI ATSGRTPYVI GGLKYARSIG AFTIGLSCNP NCQLRPLSQI
     MIAPIVGPEI VSGSTRMKAG TATKMVLNML TTGAMIRIGK TYGNRMVDVR ATNEKLVARS
     RQMLSEIVGI SGDQAEQLLQ QCDGEVKTAI VVHIKEVSPQ TARQMLVDVD GHLSRLLATP
     SE