ID A0A0R2AXG0_9LACO Unreviewed; 297 AA.
AC A0A0R2AXG0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=FC34_GL001557 {ECO:0000313|EMBL:KRM71445.1};
OS Lacticaseibacillus brantae DSM 23927.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423727 {ECO:0000313|EMBL:KRM71445.1, ECO:0000313|Proteomes:UP000051672};
RN [1] {ECO:0000313|EMBL:KRM71445.1, ECO:0000313|Proteomes:UP000051672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23927 {ECO:0000313|EMBL:KRM71445.1,
RC ECO:0000313|Proteomes:UP000051672};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM71445.1}.
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DR EMBL; AYZQ01000004; KRM71445.1; -; Genomic_DNA.
DR RefSeq; WP_057894839.1; NZ_AYZQ01000004.1.
DR AlphaFoldDB; A0A0R2AXG0; -.
DR STRING; 1423727.FC34_GL001557; -.
DR PATRIC; fig|1423727.3.peg.1579; -.
DR OrthoDB; 9813395at2; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000051672; 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; IPR000408; Reg_chr_condens.
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; PS50012; RCC1_3; 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:UP000051672}.
FT DOMAIN 55..218
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT ACT_SITE 114
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ SEQUENCE 297 AA; 31059 MW; 119E97CFDACC1ADA CRC64;
MDITKLTTEA QNAATMNLDQ MTPLEIVTTM NAEDKKVPLA VEQQLPQIAE AVSLITAAFK
QGGRLFYIGA GTSGRLGVLD AAECVPTFGI DPEMVQGLIA GGQQAMTTAV EGAEDSLSLA
QSDLEARHLN AKDIVVGIAA SGRTPYVIGG LQFAQKNGVK TVALSCNANA EISAFGDVAI
EVVPGPEILS GSTRLKSGTA QKMVLNMLST ASMVGIGKTY GNLMVDVRPT NEKLVQRAKN
IIMQITHVDE ATAGQALNAA DQSVKLAIVM LMTDDDIAQA AQRLEAASGF VRGAIEK
//
