ID R2XJ74_9ENTE Unreviewed; 296 AA.
AC R2XJ74;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000256|HAMAP-Rule:MF_00068};
DE Short=MurNAc-6-P etherase {ECO:0000256|HAMAP-Rule:MF_00068};
DE EC=4.2.1.126 {ECO:0000256|HAMAP-Rule:MF_00068};
DE AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase {ECO:0000256|HAMAP-Rule:MF_00068};
DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase {ECO:0000256|HAMAP-Rule:MF_00068};
GN Name=murQ {ECO:0000256|HAMAP-Rule:MF_00068};
GN ORFNames=UKC_02970 {ECO:0000313|EMBL:EOI54929.1};
OS Enterococcus gilvus ATCC BAA-350.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI54929.1, ECO:0000313|Proteomes:UP000013750};
RN [1] {ECO:0000313|EMBL:EOI54929.1, ECO:0000313|Proteomes:UP000013750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI54929.1,
RC ECO:0000313|Proteomes:UP000013750};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00068};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC {ECO:0000256|HAMAP-Rule:MF_00068}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00068}.
CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00068}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOI54929.1}.
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DR EMBL; AJDQ01000009; EOI54929.1; -; Genomic_DNA.
DR AlphaFoldDB; R2XJ74; -.
DR PATRIC; fig|1158614.3.peg.2956; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_9; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000013750; Unassembled WGS sequence.
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 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 NCBIfam; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1.
DR PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00068};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00068}.
FT DOMAIN 56..219
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT ACT_SITE 115
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ SEQUENCE 296 AA; 31550 MW; A0DF848C2C1084C8 CRC64;
MINLENLTTE RRNETTFGLD EMSVAQAVKL MNQEDHKVPD AVAEQLPQIE KVVSATIASF
KKGGRLIYMG AGTSGRLGVL DAAECVPTFG VEPEMVVGLI AGGEQAMTVA VEGAEDDAEL
GAQDLKDLQL TAKDMVIGIA ASGRTPYVIG GLDYACSIGA STGTVACNKD AAISKHAELP
IEVDCGPEFL TGSTRLKSGT AQKLILNMIS TISMIGIGKV YNNLMVDVKP TNEKLVERSK
RIIMQATDAD YETAARYFDE AAQNVKLAIV MILTDSTKEE AAEKLIQADG FVKKTI
//
