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MURQ_LACLA
ID   MURQ_LACLA              Reviewed;         297 AA.
AC   Q9CGG6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=LL1130;
GN   ORFNames=L144334;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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. {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; AE005176; AAK05228.1; -; Genomic_DNA.
DR   PIR; B86766; B86766.
DR   RefSeq; NP_267286.1; NC_002662.1.
DR   RefSeq; WP_010905775.1; NC_002662.1.
DR   AlphaFoldDB; Q9CGG6; -.
DR   SMR; Q9CGG6; -.
DR   STRING; 272623.L144334; -.
DR   PaxDb; Q9CGG6; -.
DR   EnsemblBacteria; AAK05228; AAK05228; L144334.
DR   KEGG; lla:L144334; -.
DR   PATRIC; fig|272623.7.peg.1208; -.
DR   eggNOG; COG2103; Bacteria.
DR   HOGENOM; CLU_049049_1_1_9; -.
DR   OMA; CPPTFCT; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000002196; 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; Reference proteome.
FT   CHAIN           1..297
FT                   /note="N-acetylmuramic acid 6-phosphate etherase"
FT                   /id="PRO_0000249633"
FT   DOMAIN          56..219
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        84
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   297 AA;  31982 MW;  8A35B577063DD672 CRC64;
     MIDLSTLTTE RRNNETFNLD QMTVAEALIK MNNEDKKVAF AVEEALPNIE PVISSAIEAF
     NKGGRLIYMG AGTSGRLGVL DAAECVPTFG VPATQVIGLI AGGDKAMTVS VEGAEDSLEL
     GRQDLIDLKL NENDLVLGIA ASGRTPYVIG ALDYAKEIGA KTASLSCNLN AEISKHAEFP
     IEVDCGPEFL TGSTRLKSGT AQKLILNMIS TISMIGIGKV YNNLMVDVKP TNEKLVERSK
     RIIMQATDCT YEEAEEKFIE ADQDVKLAIV MLLTDCAAEE GKTKLVRANG FVKNTLN
 
 
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