MURQ2_ENTFA
ID MURQ2_ENTFA Reviewed; 296 AA.
AC Q831R4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase 2 {ECO:0000255|HAMAP-Rule:MF_00068};
DE Short=MurNAc-6-P etherase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00068};
DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase 2 {ECO:0000255|HAMAP-Rule:MF_00068};
GN Name=murQ2 {ECO:0000255|HAMAP-Rule:MF_00068}; OrderedLocusNames=EF_2436;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(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; AE016830; AAO82154.1; -; Genomic_DNA.
DR RefSeq; NP_816084.1; NC_004668.1.
DR RefSeq; WP_002356712.1; NZ_KE136528.1.
DR AlphaFoldDB; Q831R4; -.
DR SMR; Q831R4; -.
DR STRING; 226185.EF_2436; -.
DR EnsemblBacteria; AAO82154; AAO82154; EF_2436.
DR GeneID; 60894483; -.
DR KEGG; efa:EF2436; -.
DR PATRIC; fig|226185.45.peg.1109; -.
DR eggNOG; COG2103; Bacteria.
DR HOGENOM; CLU_049049_1_1_9; -.
DR OMA; CPPTFCT; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000001415; 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 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; PF13580; SIS_2; 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..296
FT /note="N-acetylmuramic acid 6-phosphate etherase 2"
FT /id="PRO_0000249622"
FT DOMAIN 55..218
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
FT ACT_SITE 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00068"
SQ SEQUENCE 296 AA; 31757 MW; F75C9516F3DA2627 CRC64;
MNLENLTTER RNENTMGLDE MSVKEALQKM NQEDQKVAMA VGQELAAIEP VVEAIIKSFN
QGGRLIYMGA GTSGRLGVLD AAECVPTFGV EPEMVQGLIA GGQKAMTVAV EGAEDSKELG
RQDLVDLKLS ANDIVVGIAA SGRTPYVIGG LEYATTVGAA TATVACNKNA EISKYAQMPI
EVDAGPEFLT GSTRLKSGTA QKLILNMLST ISMIGIGKVY NNLMVDVKPT NEKLVERSKR
IIMEATGCSY EVAELKFVEA EENVKLAIVM ILTDSTKEEA TQKLIDGNQF IKNTLN
