ID MURQ_ENT38 Reviewed; 297 AA.
AC A4WDD1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, 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=Ent638_3047;
OS Enterobacter sp. (strain 638).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP61711.1; -; Genomic_DNA.
DR RefSeq; WP_015960041.1; NC_009436.1.
DR AlphaFoldDB; A4WDD1; -.
DR SMR; A4WDD1; -.
DR STRING; 399742.Ent638_3047; -.
DR KEGG; ent:Ent638_3047; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_6; -.
DR OrthoDB; 9813395at2; -.
DR UniPathway; UPA00342; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000230; 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 Gene3D; 1.10.8.1080; -; 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 InterPro; IPR009060; UBA-like_sf.
DR NCBIfam; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1.
DR PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR PANTHER; PTHR10088:SF5; N-ACETYLMURAMIC ACID 6-PHOSPHATE ETHERASE; 1.
DR Pfam; PF20741; GKRP-like_C; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Lyase.
FT CHAIN 1..297
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_1000057459"
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 297 AA; 30685 MW; 697E30C440180A4B CRC64;
MNLGSLVSES RNPQTMDLDA LSTFDLVTRF NQQDTLVALA VKETLPEVAK AVDAATDALK
SGGRIIYMGA GTSGRLGVLD ASECPPTFGV PHGLVLGLIA GGPGALLKAV EGAEDNQQLG
ADDLIAIHLT ANDLVVGLAA SGRTPYVIGG LEYAKQLGCT TVAISCNPVS PIAQVAAIAI
SPVVGPEALT GSTRLKSGTA QKLVLNMIST GAMVKFGKVY QNLMVDMQAT NIKLVDRACR
MVVQATGASR EEAEAALKQT DHDVKPAILM ILSGLDAAAA RAKLDAHQGF LRAALEN
//
