(data stored in SCRATCH zone)

SWISSPROT: D6XVW4_BACIE

ID   D6XVW4_BACIE            Unreviewed;       302 AA.
AC   D6XVW4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=N-acetylmuramic acid 6-phosphate etherase {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767172};
DE            Short=MurNAc-6-P etherase {ECO:0000256|HAMAP-Rule:MF_00068};
DE            EC=4.2.1.126 {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767172};
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   OrderedLocusNames=Bsel_0190 {ECO:0000313|EMBL:ADH97737.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97737.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97737.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl
CC       ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-
CC       phosphate and D-lactate. {ECO:0000256|HAMAP-Rule:MF_00068,
CC       ECO:0000256|SAAS:SAAS00767196}.
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, ECO:0000256|SAAS:SAAS01114880};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_00068, ECO:0000256|SAAS:SAAS00767189}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00068,
CC       ECO:0000256|SAAS:SAAS00767192}.
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
CC       aldehyde intermediate with (E)-stereochemistry, followed by the
CC       syn addition of water to give product. {ECO:0000256|HAMAP-
CC       Rule:MF_00068}.
CC   -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00068,
CC       ECO:0000256|SAAS:SAAS00767176}.
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DR   EMBL; CP001791; ADH97737.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0190; -.
DR   EnsemblBacteria; ADH97737; ADH97737; Bsel_0190.
DR   KEGG; bse:Bsel_0190; -.
DR   eggNOG; COG2103; LUCA.
DR   HOGENOM; HOG000084045; -.
DR   KO; K07106; -.
DR   OMA; CPPTFCT; -.
DR   BioCyc; BSEL439292:G1GLR-214-MONOMER; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000000271; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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.
DR   PANTHER; PTHR10088; PTHR10088; 1.
DR   PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
DR   Pfam; PF13580; SIS_2; 1.
DR   TIGRFAMs; TIGR00274; TIGR00274; 1.
DR   PROSITE; PS01272; GCKR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XVW4.
DR   SWISS-2DPAGE; D6XVW4.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00068,
KW   ECO:0000256|SAAS:SAAS01098713}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Kinase {ECO:0000313|EMBL:ADH97737.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00068,
KW   ECO:0000256|SAAS:SAAS00767171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000313|EMBL:ADH97737.1}.
FT   DOMAIN       57    220       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   COILED      112    132       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     85     85       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00068}.
FT   ACT_SITE    116    116       {ECO:0000256|HAMAP-Rule:MF_00068}.
SQ   SEQUENCE   302 AA;  32815 MW;  0CF5EB77FAABB507 CRC64;
     MTINLSDLTT ERRNERTKHI DQLSSFEILS MINEEDHLIA ESVKKEMKAI NNVVEVVCER
     FKKGGKLVYI GAGTSGRIGV LDAAEAPPTF RTDPEMIQAL IAGGDQAMFH AIEGAEDSKE
     QAKQDLERLN LSKDDVIIAI AASGRTPYAK GAVEYGNEIN AVTVGLSCNK GSELSALAQL
     AIEVEVGPEV ITGSTRMKAA TAQKLVLNMI STSSMILIGK IFENLMVDLK ASNHKLQERA
     KSITSAITGC SEEEVEQTLI KADFEVKPAI VMLKTGVSLV EAKEKLKQHR GFVRKAIESQ
     SK
//

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