ID I9NRM0_9FIRM Unreviewed; 292 AA.
AC I9NRM0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, 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=JBW_01142 {ECO:0000313|EMBL:AJQ26494.1};
OS Pelosinus fermentans JBW45.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1192197 {ECO:0000313|EMBL:AJQ26494.1, ECO:0000313|Proteomes:UP000005361};
RN [1] {ECO:0000313|EMBL:AJQ26494.1, ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|EMBL:AJQ26494.1,
RC ECO:0000313|Proteomes:UP000005361};
RX PubMed=26404608;
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Elias D.A., Arkin A.P.,
RA Fields M.W., Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45, a Member of a
RT Remarkably Competitive Group of Negativicutes in the Firmicutes Phylum.";
RL Genome Announc. 3:e01090-e01015(2015).
RN [2] {ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|Proteomes:UP000005361};
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Arkin A.P., Fields M.W.,
RA Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45.";
RL Submitted (FEB-2015) 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; CP010978; AJQ26494.1; -; Genomic_DNA.
DR RefSeq; WP_007957210.1; NZ_CP010978.1.
DR AlphaFoldDB; I9NRM0; -.
DR STRING; 1192197.JBW_01142; -.
DR KEGG; pft:JBW_01142; -.
DR HOGENOM; CLU_049049_1_1_9; -.
DR OrthoDB; 9813395at2; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000005361; 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 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:UP000005361}.
FT DOMAIN 48..211
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 76
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT ACT_SITE 107
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ SEQUENCE 292 AA; 31162 MW; 8AE1FB1D89D6B1D5 CRC64;
MEQWNQDTIE IDEVSTIEMV TMFNREDEKV AAAVGKCTEI ISSAIDLIVE RMVKGGRLFY
IGSGSGGKLG LLDATECPPT FGTDDNTVIG LISGGEEALS GWREDTEDDE ELAIKDLKAK
GFGGHDVLVG ISASGNTPYV ISAVSYAKDM GNKTIGICCS LSGKLESIAD VCVVVDVGPE
VIMGSTRLKA GTAQKMVLNM LSSCAMIKLG KTYQNLMVDV RPINRKLKQR VLDIITLATG
KGEAFALQAL TKAKGNAKLA ILMLTLNINA TIANALLKKH NGYLKKAIKD EA
//
