MURQ_GLOVI
ID MURQ_GLOVI Reviewed; 306 AA.
AC Q7NE68;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=glr4012;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(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; BA000045; BAC91953.1; -; Genomic_DNA.
DR RefSeq; NP_926958.1; NC_005125.1.
DR RefSeq; WP_011144000.1; NC_005125.1.
DR AlphaFoldDB; Q7NE68; -.
DR SMR; Q7NE68; -.
DR STRING; 251221.35214586; -.
DR EnsemblBacteria; BAC91953; BAC91953; BAC91953.
DR KEGG; gvi:glr4012; -.
DR PATRIC; fig|251221.4.peg.4044; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_3; -.
DR InParanoid; Q7NE68; -.
DR OMA; CPPTFCT; -.
DR OrthoDB; 1100044at2; -.
DR PhylomeDB; Q7NE68; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000000557; 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..306
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_0000249627"
FT DOMAIN 60..223
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 119
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ SEQUENCE 306 AA; 31768 MW; 9FD549367912C279 CRC64;
MDERLPERAH LVTEQVNPDS ARLDRLDSPS LVELFCREDE RVVPAVRAAA PAIARAIDLT
AAALRGGGRL FYVGAGTSGR LGVLDASECP PTFCTDPEQV QGIIAGGTAA LTRSVEGAED
DPEAGAAELA GRALSAADVV VGISAGGTAP YVSGALAYAR SLGGVTIFVA CVPTNQIPER
WDIEIRVPVG PEVLAGSTRL KAGTATKLVL NILSTGAMVR LGKTYGNLMV DVAVSNQKLR
DRAVRILTTL TELERTAALA LLEASGLRVK VALLMHWSNQ DPASCATALE AAGGLLPVAL
EKLSGR
