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}.
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; 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