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Database: UniProt
Entry: V5EMC7_9LACO
LinkDB: V5EMC7_9LACO
Original site: V5EMC7_9LACO 
ID   V5EMC7_9LACO            Unreviewed;       299 AA.
AC   V5EMC7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=Lc367_1373 {ECO:0000313|EMBL:EST03049.1};
OS   Lactobacillus crispatus EM-LC1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1328863 {ECO:0000313|EMBL:EST03049.1, ECO:0000313|Proteomes:UP000017999};
RN   [1] {ECO:0000313|EMBL:EST03049.1, ECO:0000313|Proteomes:UP000017999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM-LC1 {ECO:0000313|EMBL:EST03049.1,
RC   ECO:0000313|Proteomes:UP000017999};
RX   PubMed=24356836;
RA   Power S.E., Harris H.M., Bottacini F., Ross R.P., O'Toole P.W.,
RA   Fitzgerald G.F.;
RT   "Draft Genome Sequence of Lactobacillus crispatus EM-LC1, an Isolate with
RT   Antimicrobial Activity Cultured from an Elderly Subject.";
RL   Genome Announc. 1:e01070-13(2013).
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:EST03049.1}.
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DR   EMBL; AXLM01000040; EST03049.1; -; Genomic_DNA.
DR   RefSeq; WP_023488690.1; NZ_AXLM01000040.1.
DR   AlphaFoldDB; V5EMC7; -.
DR   PATRIC; fig|1328863.3.peg.1486; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000017999; 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}.
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   299 AA;  31885 MW;  A981684A96B444E1 CRC64;
     MSLENLTTEQ RNKNTMHIDS MSTLDMVKTI NEEDKKVAEA VGTQDEEIAQ AIDIGSARYQ
     QGGRLIYIGA GTSGRLGVLD AAELVPTYGI KPERAIGLIA GGKGAMYVAV EGAEDDPKLA
     AEDLKKLDLS EKDVVIGLAA SGRTPYVIGG LDYAQKVGAA TIAIACVKHS LIGQHANIAI
     EAVTGAEVVT GSTRMKAGTA QKMILNMIST GIMIRQGKVY QNVMIDVLPT NEKLVERAER
     IIQTTTNVSL EKAAKILRDA DKDVGLAIVM AKTGLAKEKA ELLLKEHENN VSSVLKENN
//
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