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Entry: A0A1D8T8Q0_9NOCA
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ID   A0A1D8T8Q0_9NOCA        Unreviewed;       310 AA.
AC   A0A1D8T8Q0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=BFN03_18600 {ECO:0000313|EMBL:AOW93994.1};
OS   Rhodococcus sp. WMMA185.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW93994.1, ECO:0000313|Proteomes:UP000178767};
RN   [1] {ECO:0000313|EMBL:AOW93994.1, ECO:0000313|Proteomes:UP000178767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMA185 {ECO:0000313|EMBL:AOW93994.1,
RC   ECO:0000313|Proteomes:UP000178767};
RA   Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT   "Draft Genome of Rhodococcus sp. WMMA185.";
RL   Submitted (AUG-2016) 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; CP017014; AOW93994.1; -; Genomic_DNA.
DR   RefSeq; WP_070380251.1; NZ_CP017014.1.
DR   AlphaFoldDB; A0A1D8T8Q0; -.
DR   STRING; 679318.BFN03_18600; -.
DR   KEGG; rhw:BFN03_18600; -.
DR   OrthoDB; 9813395at2; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000178767; 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:UP000178767}.
FT   DOMAIN          60..223
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        88
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00068"
SQ   SEQUENCE   310 AA;  31211 MW;  DD505AAC3558B34D CRC64;
     MTDLDHELAQ LATERTRPEL SGLDTRSTRD LVAAIAEDDA GVPAAVAAAS DAITAAVDVV
     VERLERGGRL VYAGAGTPGR LGVLDAAECV PTFGTEPGQV TALLAGGVDA MTASREGAED
     DPGAAAEALA DIEIGADDVL VAITASGRTP YALGAAETAR ESGAATIGIS NNAGSRLSSL
     VDVAIEVCTG PEIIAGSTRM KAGTAQKLVL NTLTTASMIR LGKTYDNLMV DVQATNDKLR
     SRAQRIVVEA TGVSPDVAAD TLAAAGGHVK TAIVALLAEI DVAEARNRLA ACAGRVRNAV
     DGGSGAETPT
//
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