ID   MURQ_TRIV2              Reviewed;         307 AA.
AC   Q3MGL8; Q93CJ3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=Ava_0242;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14756792; DOI=10.1046/j.1365-2958.2003.03851.x;
RA   Zahalak M., Pratte B., Werth K.J., Thiel T.;
RT   "Molybdate transport and its effect on nitrogen utilization in the
RT   cyanobacterium Anabaena variabilis ATCC 29413.";
RL   Mol. Microbiol. 51:539-549(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAL02107.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF408411; AAL02107.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000117; ABA19868.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MGL8; -.
DR   SMR; Q3MGL8; -.
DR   STRING; 240292.Ava_0242; -.
DR   EnsemblBacteria; ABA19868; ABA19868; Ava_0242.
DR   KEGG; ava:Ava_0242; -.
DR   eggNOG; COG2103; Bacteria.
DR   HOGENOM; CLU_049049_1_1_3; -.
DR   OMA; CPPTFCT; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000002533; 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.
FT   CHAIN           1..307
FT                   /note="N-acetylmuramic acid 6-phosphate etherase"
FT                   /id="PRO_0000249602"
FT   DOMAIN          59..222
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        87
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT   CONFLICT        17
FT                   /note="P -> L (in Ref. 1; AAL02107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77..78
FT                   /note="SG -> GS (in Ref. 1; AAL02107)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  32749 MW;  D76439633240A328 CRC64;
     MANLQERGHL LTEQVNPLSQ NLDQLSSLEL VELFNSEDRK TIEAVAAAKV QIATAIEQTA
     DRLRQGGRLF YVGAGTSGRL GVLDAAECPP TFCTPPELVQ GIIAGGAGAL VRSSEDLEDR
     AEDGDAAIAQ RHITQLDVVV GITAGGTTPF VQGAINSARQ RGALTIFIAC VPAEQVSFTA
     DIDIRLLTGP EILAGSTRLK AGTVTKLTLN ILSTGVMVKL GKVYGNRMVD VAVTNQKLRD
     RALRILEDLT GLSREAAGFL LERSGKWVKL ALVMHWTGLD KDAGDRLLSA HQGNLREAVA
     SYKNQGN