MURQ_BACTN
ID MURQ_BACTN Reviewed; 277 AA.
AC Q8ABH7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BT_0133;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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}.
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DR EMBL; AE015928; AAO75240.1; -; Genomic_DNA.
DR RefSeq; NP_809046.1; NC_004663.1.
DR RefSeq; WP_008760452.1; NC_004663.1.
DR AlphaFoldDB; Q8ABH7; -.
DR SMR; Q8ABH7; -.
DR STRING; 226186.BT_0133; -.
DR PaxDb; Q8ABH7; -.
DR PRIDE; Q8ABH7; -.
DR EnsemblBacteria; AAO75240; AAO75240; BT_0133.
DR GeneID; 60926099; -.
DR KEGG; bth:BT_0133; -.
DR PATRIC; fig|226186.12.peg.130; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_10; -.
DR InParanoid; Q8ABH7; -.
DR OMA; CPPTFCT; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IBA:GO_Central.
DR GO; GO:0016803; F:ether hydrolase activity; IBA:GO_Central.
DR GO; GO:0046348; P:amino sugar catabolic process; IBA:GO_Central.
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 GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
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; PF01380; SIS; 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; Reference proteome.
FT CHAIN 1..277
FT /note="N-acetylmuramic acid 6-phosphate etherase"
FT /id="PRO_0000249614"
FT DOMAIN 53..216
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ SEQUENCE 277 AA; 30334 MW; 088DE835CD4F8B2B CRC64;
MEFIKITEQP SLYDDLDKKS VKEILEDINT EDHKVADAVQ KAIPQIEKLV TLIIPRVKKG
GRIFYMGAGT SGRLGVLDAS EIPPTFGMPP TVVIGLIAGG DTALRNPVEN AEDDMSRGWE
ELLQHHINSE DTVIGIAASG TTPYVIGAMR TAREHGILTG CITSNPNSPM ATEADVPIEV
IVGPEYVTGS SRMKSGTAQK MILNMISTTI MIELGRVQGN KMVNMQLSNQ KLIDRGTRMI
IEELHLDYEK AEALLLLHGS VKSAIEAYRR HNSTQQE
