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MURQ_CALS4
ID   MURQ_CALS4              Reviewed;         306 AA.
AC   Q8RD35;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=TTE0212;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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; AE008691; AAM23513.1; -; Genomic_DNA.
DR   RefSeq; WP_009609599.1; NC_003869.1.
DR   AlphaFoldDB; Q8RD35; -.
DR   SMR; Q8RD35; -.
DR   STRING; 273068.TTE0212; -.
DR   EnsemblBacteria; AAM23513; AAM23513; TTE0212.
DR   KEGG; tte:TTE0212; -.
DR   eggNOG; COG2103; Bacteria.
DR   HOGENOM; CLU_049049_1_1_9; -.
DR   OMA; TRNPATM; -.
DR   OrthoDB; 1100044at2; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000000555; 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..306
FT                   /note="N-acetylmuramic acid 6-phosphate etherase"
FT                   /id="PRO_0000214840"
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   306 AA;  33209 MW;  AB84F465DE75CD31 CRC64;
     MTLEELITEG RNPNTMDIDR LSTVDMLKKI NEEDKKVPLA VEKVIPSIAE AIDRIVPRMK
     KGGRLIYVGA GTSGRIGILD ASECPPTFGV DPGLVVGIIA GGDSAIRNAI ESAEDDVEGG
     RQDLVNINLT ERDSVIGISA SGRTPYVIGA LRYAKEVGAL TIGLFCNENK NVENIVDVMI
     TPIVGPEVIM GSTRMKAGTA QKLVLNMIST GVMIKLGKVY SNLMVDLQAS NEKLRERARR
     MVKLATGAKE DLIERVLNET NYNVKLAILM IVGDMEKEKA QKLLEMADGY IAEAIKLKDL
     VLQGEE
 
 
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