ID A0A1M5K297_9BACI Unreviewed; 304 AA.
AC A0A1M5K297;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216225_10359 {ECO:0000313|EMBL:SHG46871.1};
OS Ornithinibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Ornithinibacillus.
OX NCBI_TaxID=930117 {ECO:0000313|EMBL:SHG46871.1, ECO:0000313|Proteomes:UP000183988};
RN [1] {ECO:0000313|EMBL:SHG46871.1, ECO:0000313|Proteomes:UP000183988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10683 {ECO:0000313|EMBL:SHG46871.1,
RC ECO:0000313|Proteomes:UP000183988};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQVW01000035; SHG46871.1; -; Genomic_DNA.
DR RefSeq; WP_072891297.1; NZ_FQVW01000035.1.
DR AlphaFoldDB; A0A1M5K297; -.
DR STRING; 930117.SAMN05216225_10359; -.
DR OrthoDB; 9813395at2; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000183988; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000183988}.
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 304 AA; 32801 MW; FEB47C6692523C2A CRC64;
MNKLSTLTTE MRNEKSVAID SMSTIDILKT INEEDMTVAQ SVQQVLSEIE KTVEVIYEQL
KQGGRLFYVG AGTSGRIGIM DAVECPPTYS TSPEVVQAVM AGGTKAIEKA VEGAEDSEEL
GANDLKERNL TELDVVIGIA ASGRTPYVVG ALQYANKIGA STVSLTSNTN SIISKHADIK
IEVVTGPEVL TGSTRMKAAT AHKMILNMIT TTSMIKIGKV YENLMVDLKV SNLKLKERAK
SIVSTITGST YDIAEQTLEC TNYEVKPAIV MIKTGITLEE AKYYIKEADG FVRQAIELAT
EGGN
//
